This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4h30

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4h30| PDB=4h30 | SCENE= }}
 +
===Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.===
 +
{{ABSTRACT_PUBMED_23567804}}
-
The entry 4h30 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==
-
 
+
[[4h30]] is a 2 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=4H30 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 inhibtior complex]]
 +
[[Category: Metzincin]]
 +
[[Category: Zinc protease]]

Revision as of 11:28, 24 April 2013

Template:STRUCTURE 4h30

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

4h30 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools