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FOR THE RECORD

Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtusa

¹ Instituto de Biomedicina de Valencia, C.S.I.C., 46010 Valencia, Spain
² Departamento de Química Física, Universitat de València, 46100 Burjassot (Valencia), Spain
³ Temple University College of Science and Technology, Biotechnology Center, Philadelphia, Pennsylvania 19122-6078, USA

Reprint requests to: Cezary Marcinkiewicz, Temple University College of Science and Technology, Biotechnology Center, 1900 North Broad St., Philadelphia, PA 19122-6078, USA; e-mail: cmarcink{at}nimbus.temple.edu; fax: (215) 204-6646; or Juan J. Calvete, Instituto de Biomedicina de Valencia, Jaime Roig 11, E-46010 Valencia, Spain; e-mail: jcalvete{at}ibv.csic.es; fax: 34 (96) 369 0800.

Disintegrins represent a group of cysteine-rich peptides occurring in Crotalidae and Viperidae snake venoms, and are potent antagonists of several integrin receptors. A novel disintegrin, obtustatin, was isolated from the venom of the Vipera lebetina obtusa viper, and represents the first potent and selective inhibitor of the binding of integrin ₁ß₁ to collagen IV. The primary structure of obtustatin contains 41 amino acids and is the shortest disintegrin described to date. Obtustatin shares the pattern of cysteines of other short disintegrins. However, in contrast to known short disintegrins, the integrin-binding loop of obtustatin is two residues shorter and does not express the classical RGD sequence. Using synthetic peptides, a KTS motif was identified as the integrin-binding sequence. A three-dimensional model of obtustatin, built by homology-modeling structure calculations using different templates and alignments, strongly indicates that the novel KTS motif may reside at the tip of a flexible loop.

Keywords: Disintegrin obtustatin; Vipera lebetina obtusa venom; amino acid sequence; non-RGD integrin antagonist; homology modeling

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