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Allosteric intermediates indicate R2 is the liganded hemoglobin end state.

Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG
Proc Natl Acad Sci U S A 94 7841-4 (1997)
Related entries: 1hac, 1sdk, 1sdl

Cited: 21 times
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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.

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Articles - 1hab mentioned but not cited (1)

  1. Allosteric intermediates indicate R2 is the liganded hemoglobin end state. Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG. Proc. Natl. Acad. Sci. U.S.A. 94 7841-7844 (1997)


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  2. Coarse-grained and all-atom modeling of structural states and transitions in hemoglobin. Tekpinar M, Zheng W. Proteins 81 240-252 (2013)
  3. Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters. Garcia GA, Cohen SI, Dobson CM, Knowles TP. Phys Rev E Stat Nonlin Soft Matter Phys 89 032712 (2014)
  4. What is the true structure of liganded haemoglobin? Tame JR. Trends Biochem. Sci. 24 372-377 (1999)
  5. A survey of hemoglobin quaternary structures. Dey S, Chakrabarti P, Janin J. Proteins 79 2861-2870 (2011)
  6. Crystal structure of Lysbeta(1)82-Lysbeta(2)82 crosslinked hemoglobin: a possible allosteric intermediate. Fernandez EJ, Abad-Zapatero C, Olsen KW. J. Mol. Biol. 296 1245-1256 (2000)
  7. Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (alpha2 epsilon2) haemoglobin at 2.9 A resolution. Sutherland-Smith AJ, Baker HM, Hofmann OM, Brittain T, Baker EN. J. Mol. Biol. 280 475-484 (1998)
  8. Entropy-driven intermediate steps of oxygenation may regulate the allosteric behavior of hemoglobin. Bucci E, Gryczynski Z, Razynska A, Kwansa H. Biophys. J. 74 2638-2648 (1998)
  9. Structure of the altitude adapted hemoglobin of guinea pig in the R2-state. Pairet B, Jaenicke E. PLoS ONE 5 e12389 (2010)
  10. Dynamical differences of hemoglobin and the ionotropic glutamate receptor in different states revealed by a new dynamics alignment method. Tobi D. Proteins 85 1507-1517 (2017)
  11. Structure of Greyhound hemoglobin: origin of high oxygen affinity. Bhatt VS, Zaldívar-López S, Harris DR, Couto CG, Wang PG, Palmer AF. Acta Crystallogr. D Biol. Crystallogr. 67 395-402 (2011)
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  13. Structure of liganded T-state haemoglobin from cat (Felis silvestris catus), a low oxygen-affinity species, in two different crystal forms. Balasubramanian M, Sathya Moorthy P, Neelagandan K, Ramadoss R, Kolatkar PR, Ponnuswamy MN. Acta Crystallogr. D Biol. Crystallogr. 70 1898-1906 (2014)
  14. Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans. Sundaresan SS, Ramesh P, Shobana N, Vinuchakkaravarthy T, Yasien S, Ponnuswamy MNG. Acta Crystallogr F Struct Biol Commun 77 113-120 (2021)
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Related citations provided by authors (1)

  1. Allosteric transition intermediates modelled by crosslinked haemoglobins.. Schumacher MA, Dixon MM, Kluger R, Jones RT, Brennan RG Nature 375 84-7 (1995)

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