4ijo: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4ijo|  PDB=4ijo  |  SCENE=  }}
===Unraveling hidden allosteric regulatory sites in structurally homologues metalloproteases===
{{ABSTRACT_PUBMED_23583775}}


The entry 4ijo is ON HOLD  until Paper Publication
==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.


Authors: Udi, Y., Fragai, M., Grossman, M., Mitternacht, S., Arad-Yellin, R., Calderone, V., Melikian, M., Toccafondi, M., Berezovsky, I.N., Luchinat, C., Sagi, I.
==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].  


Description: Unraveling hidden allosteric regulatory sites in structurally homologues metalloproteases
==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 10:37, 2 May 2013

Template:STRUCTURE 4ijo

Unraveling hidden allosteric regulatory sites in structurally homologues metalloproteasesUnraveling hidden allosteric regulatory sites in structurally homologues metalloproteases

Template:ABSTRACT PUBMED 23583775

FunctionFunction

[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 StructureAbout this Structure

4ijo is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. 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

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