1oww: Difference between revisions

Revision as of 00:53, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oww.png

Template:STRUCTURE 1oww

Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopySolution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy

Template:ABSTRACT PUBMED 14657397

About this StructureAbout this Structure

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

ReferenceReference

Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates., Gao M, Craig D, Lequin O, Campbell ID, Vogel V, Schulten K, Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14784-9. Epub 2003 Dec 1. PMID:14657397

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1oww|  PDB=1oww  |  SCENE=  }}
-'''Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy'''
+===Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy===
-==Overview==
+<!--
-Fibronectin (FN) forms fibrillar networks coupling cells to the extracellular matrix. The formation of FN fibrils, fibrillogenesis, is a tightly regulated process involving the exposure of cryptic binding sites in individual FN type III (FN-III) repeats presumably exposed by mechanical tension. The FN-III1 module has been previously proposed to contain such cryptic sites that promote the assembly of extracellular matrix FN fibrils. We have combined NMR and steered molecular dynamics simulations to study the structure and mechanical unfolding pathway of FN-III1. This study finds that FN-III1 consists of a beta-sandwich structure that unfolds to a mechanically stable intermediate about four times the length of the native folded state. Considering previous experimental findings, our studies provide a structural model by which mechanical stretching of FN-III1 may induce fibrillogenesis through this partially unfolded intermediate.
+The line below this paragraph, {{ABSTRACT_PUBMED_14657397}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14657397 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14657397}}
 ==About this Structure==
-OWW 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=1OWW OCA].
+OWW 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=1OWW OCA].
 ==Reference==
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 [[Category: Vogel, V.]]
 [[Category: Fibronectin type iii module]]
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