1BUY

HUMAN ERYTHROPOIETIN, NMR MINIMIZED AVERAGE STRUCTURE

Summary for 1BUY

• Entry DOI: 10.2210/pdb1buy/pdb
• Descriptor: PROTEIN (ERYTHROPOIETIN) (1 entity in total)
• Functional Keywords: cytokine, glycoprotein, growth factor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 18464.34

Authors

Cheetham, J.C.,Smith, D.M.,Aoki, K.H.,Stevenson, J.L.,Hoeffel, T.J.,Syed, R.S.,Egrie, J.,Harvey, T.S. (deposition date: 1998-09-08, release date: 1999-09-10, Last modification date: 2024-11-13)

Primary citation

Cheetham, J.C.,Smith, D.M.,Aoki, K.H.,Stevenson, J.L.,Hoeffel, T.J.,Syed, R.S.,Egrie, J.,Harvey, T.S.
NMR structure of human erythropoietin and a comparison with its receptor bound conformation.
Nat.Struct.Biol., 5:861-866, 1998

PubMed Abstract: 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.

PubMed: 9783743
DOI: 10.1038/2302

Experimental method

SOLUTION NMR