4ijo: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
'''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 07:37, 2 May 2013

Template:STRUCTURE 4ijo

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

  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

Proteopedia Page Contributors and Editors (what is this?)

OCA