1hac

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{{STRUCTURE_1hac| PDB=1hac | SCENE= }}
{{STRUCTURE_1hac| PDB=1hac | SCENE= }}
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'''CROSSLINKED HAEMOGLOBIN'''
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===CROSSLINKED HAEMOGLOBIN===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 9223274 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9223274}}
==About this Structure==
==About this Structure==
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[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
[[Category: Respiratory protein]]
[[Category: Respiratory protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:53:46 2008''

Revision as of 04:53, 1 July 2008

Image:1hac.png

Template:STRUCTURE 1hac

CROSSLINKED HAEMOGLOBIN

Template:ABSTRACT PUBMED 9223274

About this Structure

1HAC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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. 1997 Jul 22;94(15):7841-4. PMID:9223274

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