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Literature summary for 3.4.17.23 extracted from
- Structure analysis of the receptor binding of 2019-nCoV (2020), Biochem. Biophys. Res. Commun., 525, 135-140.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2 | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Callorhinchus milii | XP_007889845.1 | - |
- |
| Homo sapiens | Q9BYF1 | - |
- |
| Nipponia nippon | A0A091UR55 | - |
- |
| Paguma larvata | Q56NL1 | - |
- |
| Protobothrops mucrosquamatus | XP_029140508.1 | - |
- |
| Rhinolophus sinicus | E2DHI7 | - |
- |
| Xenopus laevis | XP_018104311.1 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| intestine | predominantly expressed in intestines, testis, and kidney | Homo sapiens | - |
| kidney | predominantly expressed in intestines, testis, and kidney | Homo sapiens | - |
| lung | expression level of ACE2 in the lung is minimal | Homo sapiens | - |
| testis | predominantly expressed in intestines, testis, and kidney | Homo sapiens | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ACE2 | - |
Homo sapiens |
| ACE2 | - |
Paguma larvata |
| ACE2 | - |
Rhinolophus sinicus |
| ACE2 | - |
Nipponia nippon |
| ACE2 | - |
Protobothrops mucrosquamatus |
| ACE2 | - |
Xenopus laevis |
| ACE2 | - |
Callorhinchus milii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| drug target | antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2 | Homo sapiens |
| evolution | ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively | Homo sapiens |
| evolution | ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively | Paguma larvata |
| evolution | ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively | Rhinolophus sinicus |
| evolution | ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively | Nipponia nippon |
| evolution | ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively | Protobothrops mucrosquamatus |
| evolution | ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively | Xenopus laevis |
| evolution | ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively | Callorhinchus milii |
| physiological function | the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus | Homo sapiens |
| physiological function | the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus | Paguma larvata |
| physiological function | the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus | Rhinolophus sinicus |
| physiological function | the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus | Nipponia nippon |
| physiological function | the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus | Protobothrops mucrosquamatus |
| physiological function | the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus | Xenopus laevis |
| physiological function | the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus | Callorhinchus milii |
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