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Literature summary for 3.4.24.7 extracted from

  • Karabencheva-Christova, T.G.; Christov, C.Z.; Fields, G.B.
    Collagenolytic matrix metalloproteinase structure-function relationships insights from molecular dynamics studies (2017), Adv. Protein Chem. Struct. Biol., 109, 1-24 .
    View publication on PubMed
Search for more literature for 3.4.24.7

Protein Variants

Protein Variants Comment Organism
E200A catalytically inactive, but correctly folded mutant enzyme. MMP-1(Glu200Ala) has an intact HPX domain. The mutant can orient and help unwind the collagen triple helix, while the catalytic MMP-1 domain (MMP-1 CAT) cleaves the triple helix Homo sapiens
L338A/H339A site-directed mutagenesis, the mutant shows an increased collagenase activity, the MMP-1 L338A/H339A mutant corresponds to the appearance of a unique anticorrelated motion and decreased correlated motions Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Collagen type III + H2O Homo sapiens ability of MMP-1 to unwind triple-helical collagen ?
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P03956
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Collagen type III + H2O ability of MMP-1 to unwind triple-helical collagen Homo sapiens ?
-
 ?
Collagen type III + H2O ability of MMP-1 to unwind triple-helical collagen. After binding the triple helix, the CAT domain can reorient to properly face the cleavage site. The dual Arg electrostatic ruler motif is modeled to be exposed in the type III collagen fibril. The two Arg residues found in type III collagen are conserved in the P5' and P17' subsites of types I and II collagen Homo sapiens ?
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 ?
additional information MMP-1 preferentially binds the alpha2(I) chain Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
collagenolytic matrix metalloproteinase
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 Homo sapiens
MMP-1
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 Homo sapiens

General Information

General Information Comment Organism
malfunction the catalytically domain of MMP-1 (MMP-1 CAT) alone does not cleave collagen Homo sapiens
additional information ability of MMP-1 to unwind triple-helical collagen, collagenolytic matrix metalloproteinase structure-function relationships, molecular dynamics studies, overview. Conformational selection mechanism for collagenolysis with full-length MMPs. Dynamic crosscorrelation analysis of MMP-1 with THP, modelling. Molecular dynamics simulations are utilized to dock MMP-1 with the cleavage site region in type III collagen Homo sapiens