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Preferential antagonism of the interactions of the integrin alpha IIb beta 3 with immobilized glycoprotein ligands by snake-venom RGD (Arg-Gly-Asp) proteins. Evidence supporting a functional role for the amino acid residues flanking the tripeptide RGD in determining the inhibitory properties of snake-venom RGD proteins.
Lu X, Williams JA, Deadman JJ, Salmon GP, Kakkar VV, Wilkinson JM, Baruch D, Authi KS, Rahman S. Lu X, et al. Among authors: rahman s. Biochem J. 1994 Dec 15;304 ( Pt 3)(Pt 3):929-36. doi: 10.1042/bj3040929. Biochem J. 1994. PMID: 7529494 Free PMC article.
Differential recognition of snake venom proteins expressing specific Arg-Gly-Asp (RGD) sequence motifs by wild-type and variant integrin alphaIIbbeta3: further evidence for distinct sites of RGD ligand recognition exhibiting negative allostery.
Rahman S, Flynn G, Aitken A, Patel Y, Hussain F, Lu X, Loftus JC, French D, Wijelath E, Strand K, Savidge GF. Rahman S, et al. Biochem J. 2000 Feb 1;345 Pt 3(Pt 3):701-9. Biochem J. 2000. PMID: 10642531 Free PMC article.
Because of the absence of structural data for integrin complexes with bound ligand, the molecular basis for this specificity modulation remains obscure. In a previous paper [Rahman, Lu, Kakkar and Authi (1995) Biochem. J. 312, 223-232] we demonstrated that two genetically …
Because of the absence of structural data for integrin complexes with bound ligand, the molecular basis for this specificity modulation rema …
4,744 results