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一氧化碳血红蛋白伊普西兰蒂的四级结构。

The quaternary structure of carbonmonoxy hemoglobin ypsilanti.

作者信息

Janin J, Wodak S J

机构信息

Laboratoire de Biologie Structurale UMR 9920-CNRS, Université Paris-Sud, Orsay, France.

出版信息

Proteins. 1993 Jan;15(1):1-4. doi: 10.1002/prot.340150102.

DOI:10.1002/prot.340150102
PMID:8451234
Abstract

We present a geometric analysis of the allosteric interface in the new Y state quaternary structure observed in liganded mutant hemoglobin Ypsilanti (beta 99 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 alpha beta 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.

摘要

我们对史密斯（Smith, F.R.）、拉特曼（Lattman, E.E.）、卡特（Carter, C.W., Jr.）（《蛋白质》10:81 - 91, 1991年）在配体化突变血红蛋白伊普西兰蒂（β99天冬氨酸→酪氨酸）中观察到的新Y态四级结构的变构界面进行了几何分析。经典的T态到R态四级结构变化是αβ二聚体围绕一条大致平行于假对称二聚体轴的轴旋转，而新的四级结构是通过对R态施加围绕与第一条轴正交的轴的额外旋转而获得的。这表明Y是一种修饰的R态，而不是T态到R态途径上的中间体。旨在模拟四级结构变化的计算机对接实验支持了这一观点。

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