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Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Will...

Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Will...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2695068

Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor

About this item

Full title

Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2009-06, Vol.106 (23), p.9226-9231

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

The lengths of von Willebrand factor (VWF) concatamers correlate with hemostatic potency. After secretion in plasma, length is regulated by hydrodynamic shear force-dependent unfolding of the A2 domain, which is then cleaved by a specific protease. The 1.9-Å crystal structure of the A2 domain demonstrates evolutionary adaptations to this shear sens...

Alternative Titles

Full title

Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2695068

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2695068

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0903679106

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