1HAC

CROSSLINKED HAEMOGLOBIN

Summary for 1HAC

• Entry DOI: 10.2210/pdb1hac/pdb
• Descriptor: HEMOGLOBIN A, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (6 entities in total)
• Functional Keywords: heme, oxygen transport, respiratory protein, erythrocyte
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 64875.28

Authors

Schumacher, M.A.,Dixon, M.M.,Kluger, R.,Jones, R.T.,Brennan, R.G. (deposition date: 1996-03-13, release date: 1997-11-12, Last modification date: 2024-11-20)

Primary citation

Schumacher, M.A.,Zheleznova, E.E.,Poundstone, K.S.,Kluger, R.,Jones, R.T.,Brennan, R.G.
Allosteric intermediates indicate R2 is the liganded hemoglobin end state.
Proc.Natl.Acad.Sci.USA, 94:7841-7844, 1997

PubMed Abstract: 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.

PubMed: 9223274
DOI: 10.1073/pnas.94.15.7841

Experimental method

X-RAY DIFFRACTION (2.6 Å)