Structure of relaxed-state human hemoglobin: insight into ligand uptake, transport and release

Joy D. Jenkins; Faik N. Musayev; Richmond Danso Danquah

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Structure of relaxed-state human hemoglobin: insight into ligand uptake, transport and release

机译：放松的状态结构人类血红蛋白:了解配体吸收、运输和释放

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Hemoglobin was one of the first protein structures to be determined by X-ray crystallography and served as a basis for the two-state MWC model for the mechanism of allosteric proteins. Since then, there has been an ongoing debate about whether Hb allostery involves the unliganded tense T state and the liganded relaxed R state or whether it involves the T state and an ensemble of liganded relaxed states. In fact, the former model is inconsistent with many functional observations, as well as the recent discoveries of several relaxed-state Hb structures such as RR2, R3 and R2.

机译：血红蛋白是第一个蛋白质结构是由x射线晶体学和决定作为两国还提供了模型基础别构蛋白的机理。已经有一个正在进行的讨论是否Hb变构效应包括T unliganded紧张状态和配体放松还是R状态涉及到T州和配体的一个整体放松的状态。不符合许多功能的观察,最近发现的几个放松的状态如RR2 Hb结构,R3和R2。

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《Acta crystallographica.Section D. Biological crystallography》 |2009年第1期|41-48|共8页
作者
Joy D. Jenkins; Faik N. Musayev; Richmond Danso Danquah;
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作者单位

Department of Medicinal Chemistry, School of Pharmacy and Institute for Structural Biology and Drug Discovery, Virginia Commonwealth University, Richmond, VA 23219, USA;

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原文格式 PDF
正文语种英语
中图分类化学;
关键词
Functional finding; Inconsistent; X-ray crystallographyInsightNervousnessHemoglobins;

机译：功能找到;矛盾;x射线crystallographyInsightNervousnessHemoglobins;

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Structure of relaxed-state human hemoglobin: insight into ligand uptake, transport and release

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