CRYSTALLOGRAPHIC REFINEMENT OF HUMAN SERUM RETINOL BINDING-PROTEIN AT 2A RESOLUTION

被引：313

作者：

COWAN, SW

NEWCOMER, ME

JONES, TA

机构：

[1] BIOMED CTR,DEPT MOLEC BIOL,BOX 590,S-75124 UPPSALA,SWEDEN

[2] VANDERBILT UNIV,MED CTR,SCH MED,DEPT BIOCHEM,NASHVILLE,TN 37232

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1990年 / 8卷 / 01期

关键词：

protein structure; RBP; RBP family;

D O I：

10.1002/prot.340080108

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：

Human serum retinol binding protein (RBP) in complex with retinol has been crystallographically refined to an R‐factor of 18.1% with 2Å resolution data. The protein topology results in an anti‐parallel β‐barrel that encapsulates the retinol ligand. A detailed description of the protein and the binding site is provided. Our structural work has helped to define a family of proteins, many of which are carrier proteins for smaller ligand molecules. We describe the structural basis for the conservation of sequence within the family. Copyright © 1990 Wiley‐Liss, Inc.

引用

页码：44 / 61

页数：18

共 100 条

[1] MOLECULAR-DYNAMICS SIMULATIONS OF THE HOLO AND APO FORMS OF RETINOL BINDING-PROTEIN - STRUCTURAL AND DYNAMIC CHANGES INDUCED BY RETINOL REMOVAL [J].