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Solution structure of a biologically active cyclic LDV peptide analogue containing a type II' beta-turn mimetic.
Doyle, P M; Harris, J C; Moody, C M; Sadler, P J; Sims, M; Thornton, J M; Uppenbrink, J; Viles, J H.
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  • Doyle PM; Wellcome Research Laboratories, Wellcome Foundation Ltd, Beckenham, Kent, UK.
Int J Pept Protein Res ; 47(6): 427-36, 1996 Jun.
Article en En | MEDLINE | ID: mdl-8836770
The solution structure of cyclo-[Gly-Leu-Asp-Val-BTD] (BTD = beta-turn dipeptide) has been determined by two-dimensional 1H-NMR (nuclear magnetic resonance) spectroscopy and systematic conformational searching combined with molecular dynamics studies. The structure contains two hydrogen bonds between the Gly and Val residues, and a type I beta-turn with Leu and Asp at the (i + 1) and (i + 2) positions of the turn. The cyclic compound shows activity in a scintillation proximity assay (SPA) for the inhibition of the interaction between the integrin alpha 4 beta 1 and vascular cell adhesion molecule-1 (VCAM-I). The structure-activity relationship of the LDV sequence is discussed.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos Cíclicos / Integrinas / Receptores Mensajeros de Linfocitos Idioma: En Revista: Int J Pept Protein Res Año: 1996 Tipo del documento: Article Pais de publicación: Dinamarca
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos Cíclicos / Integrinas / Receptores Mensajeros de Linfocitos Idioma: En Revista: Int J Pept Protein Res Año: 1996 Tipo del documento: Article Pais de publicación: Dinamarca