Crystallographic analysis of a full-length streptavidin with its C-terminal polypeptide bound in the biotin binding site

被引：26

作者：

Le Trong, L

Humbert, N

Ward, TR

Stenkamp, RE

机构：

[1] Univ Washington, Dept Biol Struct & Biochem, Seattle, WA 98195 USA

[2] Univ Washington, Biomol Struct Ctr, Seattle, WA 98195 USA

[3] Univ Neuchatel, Inst Chem, CH-2000 Neuchatel, Switzerland

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2006年 / 356卷 / 03期

关键词：

full-length streptavidin; crystallography; self-binding; protein/ligand interactions;

D O I：

10.1016/j.jmb.2005.11.086

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：

The structure of a full-length streptavidin has been determined at 1.7 angstrom resolution and shows that the 20 residue extension at the C terminus forms a well-ordered polypeptide loop on the surface of the tetramer. Residues 150-153 of the extension are bound to the ligand-binding site, possibly competing with exogenous ligands. The binding mode of these residues is compared with that of biotin and peptidic ligands. The observed structure helps to rationalize the observations that full-length mature streptavidin binds biotinylated macromolecules with reduced affinity. (c) 2005 Elsevier Ltd. All rights reserved.

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收藏

页码：738 / 745

页数：8

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