| pubmed-article:8289287 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8289287 | lifeskim:mentions | umls-concept:C0019046 | lld:lifeskim |
| pubmed-article:8289287 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:8289287 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8289287 | pubmed:dateCreated | 1994-2-18 | lld:pubmed |
| pubmed-article:8289287 | pubmed:abstractText | High-resolution crystal structures of the co-operative dimeric hemoglobin from the blood clam Scapharca inaequivalvis have been determined in the unliganded (deoxy) and carbon monoxide (CO) liganded states. The deoxy structure has been refined at 1.6 A resolution to an R-factor of 0.158 and the CO structure has been refined at 1.4 A resolution to an R-factor of 0.159. These structures reveal details of the structural transitions involved in co-operative ligand binding that involve only a minor rotation of subunits but very striking tertiary changes at the interface. A small number of residues in the F-helix appear to mediate co-operativity in this simple hemoglobin. The oxygen affinity of each subunit appears to be largely dictated by the disposition of phenylalanine 97, whose side-chain packs in the heme pocket in the deoxy state but is extruded towards the interface in the CO-liganded structure. Direct involvement of the ligand-binding heme group is a novel feature of the subunit interface and appears important for intersubunit communication. Ligation alters the conformation of the heme propionate groups along with two interacting residues from the symmetry-related subunit. These two residues, lysine 96 and asparagine 100, link the heme of one subunit with the F-helix of the second subunit in such a way as to influence the ligand affinity of that subunit. The interface is highly hydrated by well-ordered water molecules that are likely to be important in the stabilization of the two structures. | lld:pubmed |
| pubmed-article:8289287 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8289287 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8289287 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8289287 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8289287 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8289287 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8289287 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8289287 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8289287 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8289287 | pubmed:author | pubmed-author:RoyerW EWEJr | lld:pubmed |
| pubmed-article:8289287 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8289287 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:8289287 | pubmed:volume | 235 | lld:pubmed |
| pubmed-article:8289287 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8289287 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8289287 | pubmed:pagination | 657-81 | lld:pubmed |
| pubmed-article:8289287 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8289287 | pubmed:meshHeading | pubmed-meshheading:8289287-... | lld:pubmed |
| pubmed-article:8289287 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8289287 | pubmed:articleTitle | High-resolution crystallographic analysis of a co-operative dimeric hemoglobin. | lld:pubmed |
| pubmed-article:8289287 | pubmed:affiliation | Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605. | lld:pubmed |
| pubmed-article:8289287 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8289287 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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