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FEBS Lett. 2004 Nov 19;577(3):478-82.

Structural determinants of the selectivity of KTS-disintegrins for the alpha1beta1 integrin.

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1
Center for Neurovirology and Cancer Biology, Temple University, College of Science and Technology, 1900 N., 12th Street, Philadelphia, PA 19122, USA.

Abstract

KTS-disintegrins are a subfamily of short monomeric disintegrins that are potent and selective inhibitors of alpha1beta1 integrin. The amino acid sequence of the new KTS-disintegrin, viperistatin, differs from previously characterized obtustatin in three residues at position 24 (within the integrin binding loop), 38 (hydrophobic core) and 40 (C-terminal region). Noteworthy, viperistatin is about 25-fold more potent than obtustatin inhibiting the binding of this integrin to collagen IV. Synthetic peptides representing the full-length of integrin-binding loops of these disintegrins showed that the Leu24/Arg substitution appears to be partly responsible for the increased inhibitory activity of viperistatin over obtustatin.

PMID:
15556632
DOI:
10.1016/j.febslet.2004.10.050
[Indexed for MEDLINE]
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