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
- Udi Y, Fragai M, Grossman M, Mitternacht S, Arad-Yellin R, Calderone V, Melikian M, Toccafondi M, Berezovsky IN, Luchinat C, Sagi I. Unraveling Hidden Regulatory Sites in Structurally Homologous Metalloproteases. J Mol Biol. 2013 Apr 11. pii: S0022-2836(13)00240-4. doi:, 10.1016/j.jmb.2013.04.009. PMID:23583775 doi:10.1016/j.jmb.2013.04.009
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