Allosteric intermediates indicate R2 is the liganded hemoglobin end state.
Journal Article (Journal Article)
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.
- Schumacher, MA; Zheleznova, EE; Poundstone, KS; Kluger, R; Jones, RT; Brennan, RG
- July 22, 1997
Volume / Issue
- 94 / 15
Start / End Page
- 7841 - 7844
Pubmed Central ID
International Standard Serial Number (ISSN)
Digital Object Identifier (DOI)
- United States