TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 273, No. 17, Issue of April 24, pp. 10396 –10401, 1998 © 1998 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Crystal Structure of the von Willebrand Factor A1 Domain and Implications for the Binding of Platelet Glycoprotein Ib* (Received for publication, September 11, 1997, and in revised form, January 16, 1998) Jonas Emsley‡, Miguel Cruz§, Robert Handin§, and Robert Liddington‡¶ From the ‡Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom and §Brigham & Women’s Hospital, Hematology-Oncology Division, Boston, Massachusetts 02115 von Willebrand Factor (vWF) is a multimeric protein mediated by sequences within the first (A1 domain) and third (A3 domain) A type repeats of vWF. The A1 domain (residues that mediates platelet adhesion to exposed subendothe- lium at sites of vascular injury under conditions of high 479 –717) binds to platelet glycoprotein IbzIXzV complex (GpIb), flow/shear. The A1 domain of vWF (vWF-A1) forms the subendothelial heparans, cell surface sulfatides (reviewed in principal binding site for platelet glycoprotein Ib Ref. 3), and the non-fibrillar collagen type VI (4). The vWF-A3 (GpIb), an interaction that is tightly regulated. We re- domain contains the principal site for 
TI - Crystal Structure of the von Willebrand Factor A1 Domain and Implications for the Binding of Platelet Glycoprotein Ib
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.273.17.10396
DA - 1998-04-01
UR - https://www.deepdyve.com/lp/unpaywall/crystal-structure-of-the-von-willebrand-factor-a1-domain-and-4Q0XbXSeDy
DP - DeepDyve
ER -