4h49: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
m Protected "4h49" [edit=sysop:move=sysop]
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
'''Unreleased structure'''
{{STRUCTURE_4h49|  PDB=4h49  |  SCENE=  }}
===Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.===
{{ABSTRACT_PUBMED_23567804}}


The entry 4h49 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: Antoni, C., Stura, E.A., Vera, L., Nuti, E., Carafa, L., Cassar-Lajeunesse, E., Dive, V., Rossello, A.
==About this Structure==
 
[[4h49]] is a 4 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=4H49 OCA].  
Description: Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.
[[Category: Homo sapiens]]
[[Category: Macrophage elastase]]
[[Category: Antoni, C.]]
[[Category: Carafa, L.]]
[[Category: Cassar-Lajeunesse, E.]]
[[Category: Dive, V.]]
[[Category: Nuti, E.]]
[[Category: Rossello, A.]]
[[Category: Stura, E A.]]
[[Category: Vera, L.]]
[[Category: Carboxylic twin inhibitor]]
[[Category: Dimerisation]]
[[Category: Divalent inhibitor]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Metzincin]]
[[Category: Zinc protease]]

Revision as of 11:29, 24 April 2013

Template:STRUCTURE 4h49

Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.

Template:ABSTRACT PUBMED 23567804

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

4h49 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Proteopedia Page Contributors and Editors (what is this?)

OCA