Literature summary for 3.4.24.49 extracted from

Muniz, J.R.; Ambrosio, A.L.; Selistre-de-Araujo, H.S.; Cominetti, M.R.; Moura-da-Silva, A.M.; Oliva, G.; Garratt, R.C.; Souza, D.H.
The three-dimensional structure of bothropasin, the main hemorrhagic factor from Bothrops jararaca venom: insights for a new classification of snake venom metalloprotease subgroups (2008), Toxicon, 52, 807-816.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with the inhibitor POL647. The catalytic domain consists of a scaffold of two subdomains organized similarly to those described for other snake venom metalloproteinases, including the zinc and calcium-binding sites. The free cysteine residue Cys189 is located within a hydrophobic core and it is not available for disulfide bonding or other interactions. There is no identifiable secondary structure for the disintegrin domain, instead it is composed mostly of loops stabilized by seven disulfide bonds and by two calcium ions. The ECD region is in a loop and is structurally related to the RGD region of RGD disintegrins. The ECD motif is stabilized by the Cys277-Cys310 disulfide bond between the disintegrin and cysteine-rich domains and by one calcium ion. The side chain of Glu276 of the ECD motif is exposed to solvent and free to make interactions. The hyper-variable region described for other PIII snake venom metalloproteinases in the cysteine-rich domain, presents a well-conserved sequence in bothropasin	Bothrops jararaca

Crystallization (Comment)

Organism

in complex with the inhibitor POL647. The catalytic domain consists of a scaffold of two subdomains organized similarly to those described for other snake venom metalloproteinases, including the zinc and calcium-binding sites. The free cysteine residue Cys189 is located within a hydrophobic core and it is not available for disulfide bonding or other interactions. There is no identifiable secondary structure for the disintegrin domain, instead it is composed mostly of loops stabilized by seven disulfide bonds and by two calcium ions. The ECD region is in a loop and is structurally related to the RGD region of RGD disintegrins. The ECD motif is stabilized by the Cys277-Cys310 disulfide bond between the disintegrin and cysteine-rich domains and by one calcium ion. The side chain of Glu276 of the ECD motif is exposed to solvent and free to make interactions. The hyper-variable region described for other PIII snake venom metalloproteinases in the cysteine-rich domain, presents a well-conserved sequence in bothropasin

Bothrops jararaca

Organism

Organism	UniProt	Comment	Textmining
Bothrops jararaca	O93523	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

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Release 2023.1 (January 2023)