THE CONVERGENCE-DIVERGENCE DUALITY IN LECTIN DOMAINS OF SELECTIN FAMILY AND ITS IMPLICATIONS

被引：64

作者：

CHOU, KC

机构：

[1] Computer-Aided Drug Discovery, Upjohn Laboratories, Kalamazoo

来源：

FEBS LETTERS | 1995年 / 363卷 / 1-2期

关键词：

SELECTIN P-; L-; E-; CELL ADHESION RECEPTOR; SIALYL LEWIS(X) BINDING SITE; FUCOSE BINDING SITE;

D O I：

10.1016/0014-5793(95)00240-A

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A comparison of the three-dimensional structures of P-, L-, and E-selectin lectin domains reveals that there is a convergence-divergence duality for the 77-107 polypeptide in the three domains; i.e. part of the peptide is folded into a closely similar conformation, and part of it into a highly different one. Since the 77-107 residues are associated with the putative binding sites of the selectin family for ligands, this kind of duality might well reflect the common character of ligands to the selectin family as well as the specificity to each of their respective receptors. The finding may be of use for rationally designing selectin inhibitors with a given specificity and possible antiadhesion drugs.

引用

页码：123 / 126

页数：4

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