THE 7-STRANDED BETA-BARREL STRUCTURE OF APO-NEOCARZINOSTATIN AS COMPARED TO THE IMMUNOGLOBULIN DOMAIN

被引：15

作者：

ADJADJ, E

QUINIOU, E

MISPELTER, J

FAVAUDON, V

LHOSTE, JM

机构：

[1] U350 INSERM, Institut Curie, Biologie, 91405 Orsay Cedex

来源：

BIOCHIMIE | 1992年 / 74卷 / 9-10期

关键词：

NUCLEAR MAGNETIC RESONANCE; NEOCARZINOSTATIN; IMMUNOGLOBULIN; PROTEIN STRUCTURE;

D O I：

10.1016/0300-9084(92)90068-P

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 three-dimensional structure of apo-NCS, as revealed by proton NMR, is based on an antiparallel seven-stranded beta-barrel. This fold is frequently encountered in protein structures, especially for immunoglobulin domains. The strands forming the barrel are joined by flexible loops of which three are implicated in the ligand binding site of these proteins. In this paper a preliminary comparison is given with respect to the static and dynamic properties of both the constant beta-barrel and the active loops for apo-NCS and the variable V(H) domain of an immunoglobulin Fab' fragment.

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页码：853 / 858

页数：6

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