Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor.
Many adhesive interactions are mediated by Arg-Gly-Asp (RGD) sequences within adhesive proteins. Such RGD sequences are frequently recognized by structurally related heterodimers that are members of the integrin family of adhesion receptors. A region was found in the platelet RGD receptor, gpIIb/IIIa, to which an RGD peptide becomes chemically cross-linked. This region corresponds to residues 109 to 171 of gpIIIa. This segment is conserved among the beta subunits of the integrins (76 percent identity of sequence), indicating that it may play a role in the adhesive functions of this family of receptors.
D'Souza
S E
SE
Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.
Ginsberg
M H
MH
Burke
T A
TA
Lam
S C
SC
Plow
E F
EF
D000595:Amino Acid Sequence; D001665:Binding Sites; D001792:Blood Platelets / Q000276:immunology; D006801:Humans; D016023:Integrins; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010980:Platelet Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D011971:Receptors, Immunologic / Q000378:metabolism*; D018000:Receptors, Peptide
D016023:Integrins; D008562:Membrane Glycoproteins; D010980:Platelet Membrane Glycoproteins; D011971:Receptors, Immunologic; D018000:Receptors, Peptide; C051382:arginyl-glycyl-aspartic acid directed cell adhesion receptor