Identification in Collagen Type I of an Integrin α2β1-binding Site Containing an Essential GER Sequence
C. Graham Knight,Laurence F. Morton,David J. Onley,Anthony R. Peachey,Anthea J. Messent,Peter A. Smethurst,Danny S. Tuckwell,Richard W. Farndale,Michael J. Barnes +8 more
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TL;DR: The collagen type I-derived fragment α1(I)CB3 is known to recognize the platelet collagen receptor integrin α2β1 as effectively as the parent collagen, although it lacks platelet-aggregatory activity, so seven overlapping peptides that spontaneously assemble into triple helices are synthesized.
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About: This article is published in Journal of Biological Chemistry. The article was published on 11 Dec 1998. and is currently open access. The article focuses on the topics: Peptide sequence & Recognition sequence.
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References
Identification of a tetrapeptide recognition sequence for the alpha 2 beta 1 integrin in collagen.
TL;DR: Results indicate that the amino acid sequence DGEA serves as a recognition site for the alpha 2 beta 1 integrin complex on platelets and other cells.
425
Glycoprotein VI Is a Major Collagen Receptor for Platelet Activation: It Recognizes the Platelet-Activating Quaternary Structure of Collagen, Whereas CD36, Glycoprotein IIb/IIIa, and von Willebrand Factor Do Not
Beate E. Kehrel,S Wierwille,Kenneth J. Clemetson,O Anders,Michael Steiner,C.G. Knight,Richard W. Farndale,Minoru Okuma,Mike Barnes +8 more
TL;DR: These findings are consistent with a two-site, two-step model of collagen interaction with platelets involving recognition of specific sequences in collagen by an adhesive receptor such as alpha 2 beta 1 to arrest platelets under flow and subsequent recognition of another specific collagen sequence by an activatory receptor, namely GPVI.
345
Collagen-platelet interactions: evidence for a direct interaction of collagen with platelet GPIa/IIa and an indirect interaction with platelet GPIIb/IIIa mediated by adhesive proteins
TL;DR: A murine monoclonal antibody (6F1) is produced that blocks the interaction between platelets and collagen in the presence of Mg++, supporting a model wherein collagen can directly interact with GPIa/IIa and can indirectly interact with GPIIb/IIIa via intermediary adhesive proteins.
301
Crystal structure of the I domain from integrin alpha2beta1.
TL;DR: The crystal structure of the α-subunit of the integrin α2β1, a cell surface adhesion receptor for collagen and the human pathogen echovirus-1, was determined in this paper.
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