1cxw: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1cxw.gif|left|200px]]
{{Seed}}
[[Image:1cxw.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cxw|  PDB=1cxw  |  SCENE=  }}  
{{STRUCTURE_1cxw|  PDB=1cxw  |  SCENE=  }}  


'''THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2'''
===THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2===




==Overview==
<!--
BACKGROUND: Matrix metalloproteinase 2 (MMP-2, gelatinase A, 72 kDa type IV collagenase) has an important role in extracellular matrix degradation during cell migration and tissue remodeling. It is involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes. The enzyme cleaves several types of collagen, elastin, fibronectin and laminin. Binding to collagen is mediated by three repeats homologous to fibronectin type II modules, which are inserted in the catalytic domain in proximity to the active site. RESULTS: We have determined the NMR solution structure of the second type II module from human MMP-2 (col-2). The module exhibits a typical type II fold with two short double-stranded antiparallel beta sheets and three large loops packed around a cluster of conserved aromatic residues. Backbone amide dynamics, derived from (15)N relaxation experiments, correlate well with solvent accessibility and intramolecular hydrogen bonding. A synthetic peptide with the collagen consensus sequence, (Pro-Pro-Gly)(6), is shown to interact with the module. CONCLUSIONS: Spectral perturbations induced by (Pro-Pro-Gly)(6) binding reveal the region involved in the interaction of col-2 with collagen. The binding surface comprises exposed aromatic residues Phe21, Tyr38, Trp40, Tyr47, Tyr53 and Phe55, and the neighboring Gly33-Gly37 segment.
The line below this paragraph, {{ABSTRACT_PUBMED_10545322}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10545322 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10545322}}


==About this Structure==
==About this Structure==
1CXW is a [[Single protein]] structure of 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=1CXW OCA].  
1CXW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXW OCA].  


==Reference==
==Reference==
Line 31: Line 35:
[[Category: Alpha helix]]
[[Category: Alpha helix]]
[[Category: Beta sheet]]
[[Category: Beta sheet]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:13:45 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:44:43 2008''

Revision as of 18:44, 30 June 2008

File:1cxw.png

Template:STRUCTURE 1cxw

THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2

Template:ABSTRACT PUBMED 10545322

About this Structure

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

Reference

The second type II module from human matrix metalloproteinase 2: structure, function and dynamics., Briknarova K, Grishaev A, Banyai L, Tordai H, Patthy L, Llinas M, Structure. 1999 Oct 15;7(10):1235-45. PMID:10545322

Page seeded by OCA on Mon Jun 30 21:44:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1cxw&oldid=584787"