DETERMINATION OF THE SECONDARY STRUCTURE AND FOLDING TOPOLOGY OF AN RNA-BINDING DOMAIN OF MAMMALIAN HNRNP A1 PROTEIN USING 3-DIMENSIONAL HETERONUCLEAR MAGNETIC-RESONANCE SPECTROSCOPY

被引：47

作者：

GARRETT, DS

LODI, PJ

SHAMOO, Y

WILLIAMS, KR

CLORE, GM

GRONENBORN, AM

机构：

[1] NIDDKD, CHEM PHYS LAB, BETHESDA, MD 20892 USA

[2] YALE UNIV, SCH MED, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06510 USA

[3] YALE UNIV, SCH MED, HOWARD HUGHES MED INST, NEW HAVEN, CT 06510 USA

来源：

BIOCHEMISTRY | 1994年 / 33卷 / 10期

关键词：

D O I：

10.1021/bi00176a015

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 secondary structure and folding topology of the first RNA binding domain of the human hnRNP A1 protein was determined by multidimensional heteronuclear NMR spectroscopy. The 92 amino acid long domain exhibits a beta alpha beta beta alpha beta folding pattern, arranged in a four-stranded antiparallel beta-sheet flanked by two alpha-helices, which is very similar to that found for other members of this family. Regions of marked variation between the structurally characterized RNA binding proteins of this class to date are mainly localized in the loops connecting the secondary structure elements.

引用

页码：2852 / 2858

页数：7

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