Allosteric intermediates indicate R2 is the liganded hemoglobin end state.
Publication
, Journal Article
Schumacher, MA; Zheleznova, EE; Poundstone, KS; Kluger, R; Jones, RT; Brennan, RG
Published in: Proc Natl Acad Sci U S A
July 22, 1997
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.
Duke Scholars
Altmetric Attention Stats
Dimensions Citation Stats
Published In
Proc Natl Acad Sci U S A
DOI
ISSN
0027-8424
Publication Date
July 22, 1997
Volume
94
Issue
15
Start / End Page
7841 / 7844
Location
United States
Related Subject Headings
- Protein Conformation
- Ligands
- Humans
- Hemoglobins
- Allosteric Regulation
Citation
APA
Chicago
ICMJE
MLA
NLM
Schumacher, M. A., Zheleznova, E. E., Poundstone, K. S., Kluger, R., Jones, R. T., & Brennan, R. G. (1997). Allosteric intermediates indicate R2 is the liganded hemoglobin end state. Proc Natl Acad Sci U S A, 94(15), 7841–7844. https://doi.org/10.1073/pnas.94.15.7841
Schumacher, M. A., E. E. Zheleznova, K. S. Poundstone, R. Kluger, R. T. Jones, and R. G. Brennan. “Allosteric intermediates indicate R2 is the liganded hemoglobin end state.” Proc Natl Acad Sci U S A 94, no. 15 (July 22, 1997): 7841–44. https://doi.org/10.1073/pnas.94.15.7841.
Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG. Allosteric intermediates indicate R2 is the liganded hemoglobin end state. Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7841–4.
Schumacher, M. A., et al. “Allosteric intermediates indicate R2 is the liganded hemoglobin end state.” Proc Natl Acad Sci U S A, vol. 94, no. 15, July 1997, pp. 7841–44. Pubmed, doi:10.1073/pnas.94.15.7841.
Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG. Allosteric intermediates indicate R2 is the liganded hemoglobin end state. Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7841–7844.
Published In
Proc Natl Acad Sci U S A
DOI
ISSN
0027-8424
Publication Date
July 22, 1997
Volume
94
Issue
15
Start / End Page
7841 / 7844
Location
United States
Related Subject Headings
- Protein Conformation
- Ligands
- Humans
- Hemoglobins
- Allosteric Regulation