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|1buy, 1 NMR models ()|
HUMAN ERYTHROPOIETIN, NMR MINIMIZED AVERAGE STRUCTURE
The solution structure of human erythropoietin (EPO) has been determined by nuclear magnetic resonance spectroscopy and the overall topology of the protein is revealed as a novel combination of features taken from both the long-chain and short-chain families of hematopoietic growth factors. Using the structure and data from mutagenesis studies we have elucidated the key physiochemical properties defining each of the two receptor binding sites on the EPO protein. A comparison of the NMR structure of the free EPO ligand to the receptor bound form, determined by X-ray crystallography, reveals conformational changes that may accompany receptor binding.
NMR structure of human erythropoietin and a comparison with its receptor bound conformation., Cheetham JC, Smith DM, Aoki KH, Stevenson JL, Hoeffel TJ, Syed RS, Egrie J, Harvey TS, Nat Struct Biol. 1998 Oct;5(10):861-6. PMID:9783743
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
[EPO_HUMAN] Genetic variation in EPO is associated with susceptbility to microvascular complications of diabetes type 2 (MVCD2) [MIM:612623]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
[EPO_HUMAN] Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass.