Allosteric intermediates indicate R2 is the liganded hemoglobin end state.
Allosteric intermediates indicate R2 is the liganded hemoglobin end state.
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变构中间体表明 R2 是配体血红蛋白终态。
DOI：
10.1073/pnas.94.15.7841
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发表时间：
1997
影响因子：
11.1
通讯作者：
Brennan,RG
中科院分区：
文献类型：
--
作者：
Schumacher,MA;Zheleznova,EE;Poundstone,KS;Kluger,R;Jones,RT;Brennan,RG
血红蛋白一直是理解蛋白质变构的长期范例。在这里，两种化学交联的、完全配体的血红蛋白α2β 82CA 82 β和α2β 82ND 82 β的X射线结构分别以2.3 nm和2.6 nm的分辨率被描述。引人注目的是，这些交联血红蛋白呈现出介于R和有争议的配体血红蛋白状态R2之间的中间构象，而不是R和T之间的中间构象。因此，这些结构仅支持T ParticipR ParticipR2变构途径，并强调了R2构象的生理重要性。
Hemoglobin has been a long-standing paradigm for understanding protein allostery. Here, the x-ray structures of two chemically crosslinked, fully liganded hemoglobins, α2β82CA82β and α2β82ND82β, are described at 2.3 Å and 2.6 Å resolution, respectively. Strikingly, these crosslinked hemoglobins assume intermediate conformations that lie between those of R and the controversial liganded hemoglobin state R2 rather than between R and T. Thus, these structures support only a T ↔ R ↔ R2 allosteric pathway and underscore the physiological importance of the R2 conformation.