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| {{STRUCTURE_1sdl| PDB=1sdl | SCENE= }} | | {{STRUCTURE_1sdl| PDB=1sdl | SCENE= }} |
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| '''CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A'''
| | ===CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A=== |
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| ==Overview==
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| The structural end-points of haemoglobin's transition from its low-oxygen-affinity (T) to high-oxygen-affinity (R) state, have been well established by X-ray crystallography, but short-lived intermediates have proved less amenable to X-ray studies. Here we use chemical crosslinking to fix these intermediates for structural characterization. We describe the X-ray structures of three haemoglobins, alpha 2 beta 1S82 beta, alpha 2 beta 1Tm82 beta and alpha 2 beta 1,82Tm82 beta, which were crosslinked between the amino groups of residues beta Val1 and beta Lys82 by 3,3'-stilbenedicarboxylic acid (S) or trimesic acid (Tm) while in the deoxy state, and saturated with carbon monoxide before crystallization. alpha 2 beta 1S82 beta, which has almost normal oxygen affinity, is completely in the R-state conformation; however, alpha 2 beta 1Tm82 beta and alpha 2 beta 1,82Tm82 beta, both of which have low oxygen affinity, have been prevented from completing their transition into the R state and display many features of a transitional intermediate. These haemoglobins therefore represent a snapshot of the nascent R state. | | The line below this paragraph, {{ABSTRACT_PUBMED_7723849}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7723849 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7723849}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Polymorphism]] | | [[Category: Polymorphism]] |
| [[Category: Respiratory protein]] | | [[Category: Respiratory protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:34:46 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:03:39 2008'' |