Allosteric intermediates indicate R2 is the liganded hemoglobin end state.

Published

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.

Full Text

Duke Authors

Cited Authors

  • Schumacher, MA; Zheleznova, EE; Poundstone, KS; Kluger, R; Jones, RT; Brennan, RG

Published Date

  • July 22, 1997

Published In

Volume / Issue

  • 94 / 15

Start / End Page

  • 7841 - 7844

PubMed ID

  • 9223274

Pubmed Central ID

  • 9223274

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.94.15.7841

Language

  • eng

Conference Location

  • United States