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1hac
From Proteopedia
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CROSSLINKED HAEMOGLOBIN
Overview
Hemoglobin has been a long-standing paradigm for understanding protein, allostery. Here, the x-ray structures of two chemically crosslinked, fully, liganded hemoglobins, alpha2beta82CA82beta and alpha2beta82ND82beta, are, described at 2.3 A and 2.6 A 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 left and right, arrow R left and right arrow R2 allosteric pathway and underscore the, physiological importance of the R2 conformation.
About this Structure
1HAC is a Protein complex structure of sequences from Homo sapiens with HEM, CMO and NDD as ligands. Full crystallographic information is available from OCA.
Reference
Allosteric intermediates indicate R2 is the liganded hemoglobin end state., Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG, Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7841-4. PMID:9223274
Page seeded by OCA on Thu Nov 8 13:03:42 2007
Categories: Homo sapiens | Protein complex | Brennan, R.G. | Dixon, M.M. | Jones, R.T. | Kluger, R. | Schumacher, M.A. | CMO | HEM | NDD | Erythrocyte | Heme | Oxygen transport | Respiratory protein
