1oww: Difference between revisions
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'''Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy'''<br /> | '''Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy'''<br /> | ||
==Overview== | ==Overview== | ||
Fibronectin (FN) forms fibrillar networks coupling cells to the | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1OWW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1OWW is a [http://en.wikipedia.org/wiki/Single_protein 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Campbell, I | [[Category: Campbell, I D.]] | ||
[[Category: Craig, D.]] | [[Category: Craig, D.]] | ||
[[Category: Gao, M.]] | [[Category: Gao, M.]] | ||
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[[Category: fibronectin type iii module]] | [[Category: fibronectin type iii module]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:39 2008'' | ||
Revision as of 15:22, 21 February 2008
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Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this StructureAbout this Structure
1OWW is a Single protein structure of sequence from Homo sapiens. Full crystallographic 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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