1hac

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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

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