Allosteric Intermediates Indicate R2 is the Liganded Hemoglobin end State

Hemoglobin has been a long-standing paradigm for understanding protein allostery. Here, the x-ray structures of two chemically crosslinked, fully liganded hemoglobins, α2β82CA82β and α2β82ND82β , are described at 2.3 angstrom and 2.6 angstrom resolution, respectively. Strikingly, these crosslinked h...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1997-07, Vol.94 (15), p.7841-7844
Main Authors: Schumacher, Maria A., Zheleznova, Ekaterina E., Poundstone, Kitty S., Kluger, Ronald, Jones, Richard T., Brennan, Richard G.
Format: Article
Language:English
Subjects:
Allosteric Regulation
Atoms
Biochemistry
Biological Sciences
Coordinate systems
Dimers
Hemoglobin
Hemoglobins
Hemoglobins - chemistry
Hemoglobins - metabolism
Humans
Imidazoles
Ligands
Molecular structure
Molecules
Phosphates
Protein Conformation
Proteins
Trajectories
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Hemoglobin has been a long-standing paradigm for understanding protein allostery. Here, the x-ray structures of two chemically crosslinked, fully liganded hemoglobins, α2β82CA82β and α2β82ND82β , are described at 2.3 angstrom and 2.6 angstrom 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$\leftrightarrow $R$\leftrightarrow $R2 allosteric pathway and underscore the physiological importance of the R2 conformation.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.94.15.7841