THE QUATERNARY STRUCTURE OF CARBONMONOXYHEMOGLOBIN YPSILANTI

被引：34

作者：

JANIN, J ^{[1
]}

WODAK, SJ ^{[1
]}

机构：

[1] UNIV LIBRE BRUXELLES,UCMB,B-1050 BRUSSELS,BELGIUM

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1993年 / 15卷 / 01期

关键词：

MUTANT HEMOGLOBIN; ALLOSTERY; QUATERNARY STRUCTURE CHANGE; DOCKING;

D O I：

10.1002/prot.340150102

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：

We present a geometric analysis of the allosteric interface in the new Y state quaternary structure observed in liganded mutant hemoglobin Ypsilanti (beta99 Asp --> Tyr) by Smith, F.R., Lattman, E.E., Carter, C.W., Jr. (Proteins 10:81-91, 1991). The classical T to R quaternary structure change being a rotation of alphabeta dimers about an axis which is approximately parallel to the dimer axis of pseudosymmetry, the new quaternary structure is obtained by applying to R an additional rotation about an axis orthogonal to the first. This suggests that Y is a modified R state rather than an intermediate on the T to R pathway. Computer docking experiments designed to simulate the quaternary structure change support this suggestion.

引用

页码：1 / 4

页数：4

共 15 条

[1] EFFECTS OF SITE-SPECIFIC AMINO-ACID MODIFICATION ON PROTEIN INTERACTIONS AND BIOLOGICAL FUNCTION [J].