Safo Martin K, Ahmed Mostafa H, Ghatge Mohini S, Boyiri Telih
Department of Medicinal Chemistry, School of Pharmacy and Institute for Structural Biology and Drug Discovery, Virginia Commonwealth University, Richmond, VA 23219, USA.
Biochim Biophys Acta. 2011 Jun;1814(6):797-809. doi: 10.1016/j.bbapap.2011.02.013. Epub 2011 Mar 8.
The major physiological function of hemoglobin (Hb) is to bind oxygen in the lungs and deliver it to the tissues. This function is regulated and/or made efficient by endogenous heterotropic effectors. A number of synthetic molecules also bind to Hb to alter its allosteric activity. Our purpose is to review the current state of Hb structure and function that involves ensemble of tense and relaxed hemoglobin states and the dynamic equilibrium of the multistate due to the binding of endogenous heterotropic or synthetic allosteric effectors. The review also discusses the atomic interactions of synthetic ligands with the function or altered allosteric function of Hb that could be potentially harnessed for the treatment of diseases. This article is part of a Special Issue entitled: Protein Structure and Function in the Crystalline State.
血红蛋白（Hb）的主要生理功能是在肺部结合氧气并将其输送到组织中。该功能由内源性异促效应剂调节和/或提高效率。许多合成分子也与Hb结合以改变其别构活性。我们的目的是综述Hb结构和功能的当前状态，其涉及紧张态和松弛态血红蛋白状态的集合以及由于内源性异促或合成别构效应剂的结合导致的多态动态平衡。该综述还讨论了合成配体与Hb功能或改变的别构功能之间的原子相互作用，这些相互作用可能被用于治疗疾病。本文是名为：晶态蛋白质的结构与功能的特刊的一部分。
