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.


1su3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1su3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1su3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1su3| PDB=1su3 | SCENE= }}
{{STRUCTURE_1su3| PDB=1su3 | SCENE= }}
-
'''X-ray structure of human proMMP-1: New insights into collagenase action'''
+
===X-ray structure of human proMMP-1: New insights into collagenase action===
-
==Overview==
+
<!--
-
Vertebrate collagenases, members of the matrix metalloproteinase (MMP) family, initiate interstitial fibrillar collagen breakdown. It is essential in many biological processes, and unbalanced collagenolysis is associated with diseases such as arthritis, cancer, atherosclerosis, aneurysm, and fibrosis. These metalloproteinases are secreted from the cell as inactive precursors, procollagenases (proMMPs). To gain insights into the structural basis of their activation mechanisms and collagen binding, we have crystallized recombinant human proMMP-1 and determined its structure to 2.2 A resolution. The catalytic metalloproteinase domain and the C-terminal hemopexin (Hpx) domain show the classical MMP-fold, but the structure has revealed new features in surface loops and domain interaction. The prodomain is formed by a three-helix bundle and gives insight into the stepwise activation mechanism of proMMP-1. The prodomain interacts with the Hpx domain, which affects the position of the Hpx domain relative to the catalytic domain. This interaction results in a "closed" configuration of proMMP-1 in contrast to the "open" configuration observed previously for the structure of active MMP-1. This is the first evidence of mobility of the Hpx domain in relation to the catalytic domain, providing an important clue toward the understanding of the collagenase-collagen interaction and subsequent collagenolysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15611040}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15611040 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15611040}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:11:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:46:45 2008''

Revision as of 09:46, 28 July 2008

Image:1su3.png

Template:STRUCTURE 1su3

X-ray structure of human proMMP-1: New insights into collagenase action

Template:ABSTRACT PUBMED 15611040

About this Structure

1SU3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding., Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K, J Biol Chem. 2005 Mar 11;280(10):9578-85. Epub 2004 Dec 15. PMID:15611040

Page seeded by OCA on Mon Jul 28 12:46:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1su3"
Personal tools