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4ijo
From Proteopedia
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| - | + | {{STRUCTURE_4ijo| PDB=4ijo | SCENE= }} | |
| + | ===Unraveling hidden allosteric regulatory sites in structurally homologues metalloproteases=== | ||
| + | {{ABSTRACT_PUBMED_23583775}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/MMP12_HUMAN 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 [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJO OCA]. | ||
| - | + | ==Reference== | |
| + | <ref group="xtra">PMID:017096442</ref><references group="xtra"/><references/> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Macrophage elastase]] | ||
| + | [[Category: Arad-Yellin, R.]] | ||
| + | [[Category: Berezovsky, I N.]] | ||
| + | [[Category: Calderone, V.]] | ||
| + | [[Category: Fragai, M.]] | ||
| + | [[Category: Grossman, M.]] | ||
| + | [[Category: Luchinat, C.]] | ||
| + | [[Category: Melikian, M.]] | ||
| + | [[Category: Mitternacht, S.]] | ||
| + | [[Category: Sagi, I.]] | ||
| + | [[Category: Toccafondi, M.]] | ||
| + | [[Category: Udi, Y.]] | ||
| + | [[Category: Amphiphol]] | ||
| + | [[Category: Degradation of the extracellular matrix protein]] | ||
| + | [[Category: Extracellular]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Matrix metalloproteinase]] | ||
| + | [[Category: Regulatory site]] | ||
Revision as of 07:37, 2 May 2013
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
