Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3

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Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3

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Title: Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3
Author: Xiao, Tsan; Springer, Timothy A.; Zhu, Jianghai

Note: Order does not necessarily reflect citation order of authors.

Citation: Springer, Timothy A., Jianghai Zhu, and Tsan Xiao. 2008. Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3. The Journal of Cell Biology 182(4): 791-800.
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Abstract: Hemostasis and thrombosis (blood clotting) involve fibrinogen binding to integrin αIIbβ3 on platelets, resulting in platelet aggregation. αvβ3 binds fibrinogen via an Arg-Asp-Gly (RGD) motif in fibrinogen's α subunit. αIIbβ3 also binds to fibrinogen; however, it does so via an unstructured RGD-lacking C-terminal region of the γ subunit (γC peptide). These distinct modes of fibrinogen binding enable αIIbβ3 and αvβ3 to function cooperatively in hemostasis. In this study, crystal structures reveal the integrin αIIbβ3–γC peptide interface, and, for comparison, integrin αIIbβ3 bound to a lamprey γC primordial RGD motif. Compared with RGD, the GAKQAGDV motif in γC adopts a different backbone configuration and binds over a more extended region. The integrin metal ion–dependent adhesion site (MIDAS) Mg2+ ion binds the γC Asp side chain. The adjacent to MIDAS (ADMIDAS) Ca2+ ion binds the γC C terminus, revealing a contribution for ADMIDAS in ligand binding. Structural data from this natively disordered γC peptide enhances our understanding of the involvement of γC peptide and integrin αIIbβ3 in hemostasis and thrombosis.
Published Version: doi:10.1083/jcb.200801146
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2518716/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:4878928

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