pubmed-article:8114096 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8114096 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
pubmed-article:8114096 | lifeskim:mentions | umls-concept:C0019046 | lld:lifeskim |
pubmed-article:8114096 | lifeskim:mentions | umls-concept:C1979845 | lld:lifeskim |
pubmed-article:8114096 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:8114096 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:8114096 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:8114096 | pubmed:dateCreated | 1994-3-29 | lld:pubmed |
pubmed-article:8114096 | pubmed:abstractText | The beta-chains isolated from the human hemoglobin alpha 2 beta 2 heterotetramer self-assemble to form a beta 4 homotetramer. We report the structure of the carbonmonoxy-beta 4 (CO beta 4) tetramer refined at a resolution of 1.8 A. Compared to the three known quaternary structures of human hemoglobin, the T state, the R state and the R2 state, the quaternary structure of CO beta 4 most closely resembles the R state. While the degree of structural similarity between CO beta 4 and the R state of liganded alpha 2 beta 2 is quite high, differences between the alpha and beta-chain sequences result in interesting alternative packing arrangements at the subunit interfaces of CO beta 4. In particular, Arg40 beta and Asp99 beta interact across the CO beta 4 equivalent of the alpha 1 beta 2 interface to form two symmetry-related salt bridges that have no counterpart in either liganded or deoxyhemoglobin. Because these salt bridges are near a 2-fold symmetry axis, steric constraints prevent their simultaneous formation, and electron density images of Arg40 beta and Asp99 beta show equally populated dual conformations for the side-chains of both residues. Relative to the liganded alpha 2 beta 2 tetramer, the Arg40 beta...Asp99 beta salt bridges introduce ionic interactions that should strengthen the CO beta 4 tetramer. The CO beta 4 equivalent of the alpha 1 alpha 2 and beta 1 beta 2 interfaces strengthens the tetramer relative to the liganded alpha 2 beta 2 tetramer by tethering both ends of the central cavity. (The entrance to the central cavity is altered so that the N termini move closer together and the C termini further apart, forming an anion binding pocket that is absent in liganded alpha 2 beta 2 hemoglobin.) In contrast, analysis of the CO beta 4 counterpart of the alpha 1 beta 1 interface indicates that this interface is weakened in the CO beta 4 tetramer. These differences in interface stability provide a structural explanation for the published observation that the alpha 2 beta 2 tetramer assembles via a stable alpha 1 beta 1 dimer intermediate, whereas assembly of the CO beta 4 tetramer is characterized more accurately by a monomer-tetramer equilibrium. | lld:pubmed |
pubmed-article:8114096 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8114096 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8114096 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8114096 | pubmed:language | eng | lld:pubmed |
pubmed-article:8114096 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8114096 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8114096 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8114096 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8114096 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8114096 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8114096 | pubmed:month | Feb | lld:pubmed |
pubmed-article:8114096 | pubmed:issn | 0022-2836 | lld:pubmed |
pubmed-article:8114096 | pubmed:author | pubmed-author:ArnoneAA | lld:pubmed |
pubmed-article:8114096 | pubmed:author | pubmed-author:RogersP HPH | lld:pubmed |
pubmed-article:8114096 | pubmed:author | pubmed-author:BorgstahlG... | lld:pubmed |
pubmed-article:8114096 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8114096 | pubmed:day | 25 | lld:pubmed |
pubmed-article:8114096 | pubmed:volume | 236 | lld:pubmed |
pubmed-article:8114096 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8114096 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8114096 | pubmed:pagination | 817-30 | lld:pubmed |
pubmed-article:8114096 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:8114096 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:8114096 | pubmed:articleTitle | The 1.8 A structure of carbonmonoxy-beta 4 hemoglobin. Analysis of a homotetramer with the R quaternary structure of liganded alpha 2 beta 2 hemoglobin. | lld:pubmed |
pubmed-article:8114096 | pubmed:affiliation | Department of Biochemistry, University of Iowa, Iowa City 52242. | lld:pubmed |
pubmed-article:8114096 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8114096 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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