Abstract：
:The alpha IIb beta 3 integrin binds Arg-Gly-Asp-containing (RGD-containing) ligands in a cation-dependent interaction. A fourteen amino acid sequence, beta 3 (118-131), and an antibody to it, inhibited ligand binding functions of alpha IIb beta 3, and a 1:1 stoichiometric beta 3 (118-131)-RGD complex was detected by mass spectroscopy. Cation binding to beta 3 (118-131) was demonstrated by terbium luminescence and mass spectroscopy. Notably, ligand displaced cation from the beta 3(118-131) peptide and also from purified alpha IIb beta 3. Thus, beta 3 (118-131), a highly conserved region in integrin beta subunits, binds both ligand and cation. Formation of a ternary complex between cation, ligand, and receptor, with subsequent displacement of cation from beta 3 (118-131) and a second site within the receptor, may be central to the mechanism of ligand recognition by integrins.
journal_name
Celljournal_title
Cellauthors
D'Souza SE,Haas TA,Piotrowicz RS,Byers-Ward V,McGrath DE,Soule HR,Cierniewski C,Plow EF,Smith JWdoi
10.1016/0092-8674(94)90551-7subject
Has Abstractpub_date
1994-11-18 00:00:00pages
659-67issue
4eissn
0092-8674issn
1097-4172pii
0092-8674(94)90551-7journal_volume
79pub_type
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