TY - JOUR
T1 - Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2, CD49b/CD29)
AU - Kamata, Tetsuji
AU - Puzon, Wilma
AU - Takada, Yoshikazu
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1994/4/1
Y1 - 1994/4/1
N2 - Integrin αβ1 is a cell surface adhesion receptor for collagen and echovirus 1. Here we localized the epitopes for anti-α2 monoclonal antibodies using interspecies (human/bovine) α2 chimeras with different lengths of human α2 sequence on the amino-terminal side and site-directed mutagenesis. The antibodies that block the collagen and/or echovirus 1 binding to human α2β1 (6F1, RMAC11, 12F1, and AA10) recognizes a small region (residues 173-259) within the I domain. Asp-160 and Arg-242 are critical for binding of the two other function-inhibiting antibodies, P1H5 and 5E8, respectively. Notably, mutations of Asp-151 and Asp-254 block the binding of α2β1 to collagen. These data suggest that the I domain (residues 140-359) is critically involved in the ligand/receptor interactions, and collagen and echovirus 1 binding sites are adjacent or overlapping within the I domain. The sequence of the residues 173-259 of α2 overlap with the peptide sequences (M11 and M20) that derive from von Willebrand factor A1 and A3 domains (homologous to the α2 I domain) and block von Willebrand factor/collagen interaction, suggesting that the epitope region of α2 (residues 173-259) may really be involved in ligand recognition.
AB - Integrin αβ1 is a cell surface adhesion receptor for collagen and echovirus 1. Here we localized the epitopes for anti-α2 monoclonal antibodies using interspecies (human/bovine) α2 chimeras with different lengths of human α2 sequence on the amino-terminal side and site-directed mutagenesis. The antibodies that block the collagen and/or echovirus 1 binding to human α2β1 (6F1, RMAC11, 12F1, and AA10) recognizes a small region (residues 173-259) within the I domain. Asp-160 and Arg-242 are critical for binding of the two other function-inhibiting antibodies, P1H5 and 5E8, respectively. Notably, mutations of Asp-151 and Asp-254 block the binding of α2β1 to collagen. These data suggest that the I domain (residues 140-359) is critically involved in the ligand/receptor interactions, and collagen and echovirus 1 binding sites are adjacent or overlapping within the I domain. The sequence of the residues 173-259 of α2 overlap with the peptide sequences (M11 and M20) that derive from von Willebrand factor A1 and A3 domains (homologous to the α2 I domain) and block von Willebrand factor/collagen interaction, suggesting that the epitope region of α2 (residues 173-259) may really be involved in ligand recognition.
UR - http://www.scopus.com/inward/record.url?scp=0028225987&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028225987&partnerID=8YFLogxK
M3 - Article
C2 - 7511592
AN - SCOPUS:0028225987
SN - 0021-9258
VL - 269
SP - 9659
EP - 9663
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 13
ER -