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Structural transitions upon ligand binding in a cooperative dimeric hemoglobin | W E Royer
; W A Hendrickson
; E Chiancone
; | Date: |
3 Aug 1990 | Journal: | Science, 249 (4968), 518-21 | Abstract: | Comparison of the 2.4 angstrom resolution crystal structures of dimeric clam hemoglobin in the deoxygenated and carbon-monoxide liganded states shows how radically different the structural basis for cooperative oxygen binding is from that operative in mammalian hemoglobins. Heme groups are in direct communication across a novel subunit interface formed by the E and F helices. The conformational changes at this interface that accompany ligand binding are more dramatic at a tertiary level but more subtle at a quaternary level than those in mammalian hemoglobins. These findings suggest a cooperative mechanism that links ligation at one subunit with potentiation of affinity at the second subunit. | Source: | PubMed, pmid2382132 | Services: | Forum | Review | Favorites |
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