4ijo
From Proteopedia
Contents |
Unraveling hidden allosteric regulatory sites in structurally homologues metalloproteases
Template:ABSTRACT PUBMED 23583775
Function
[MMP12_HUMAN] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
About this Structure
4ijo is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Bertini I, Calderone V, Fragai M, Luchinat C, Maletta M, Yeo KJ. Snapshots of the reaction mechanism of matrix metalloproteinases. Angew Chem Int Ed Engl. 2006 Dec 4;45(47):7952-5. PMID:17096442 doi:10.1002/anie.200603100
Categories: Homo sapiens | Macrophage elastase | Arad-Yellin, R. | Berezovsky, I N. | Calderone, V. | Fragai, M. | Grossman, M. | Luchinat, C. | Melikian, M. | Mitternacht, S. | Sagi, I. | Toccafondi, M. | Udi, Y. | Amphiphol | Degradation of the extracellular matrix protein | Extracellular | Hydrolase | Matrix metalloproteinase | Regulatory site