| pubmed-article:15178680 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15178680 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:15178680 | lifeskim:mentions | umls-concept:C1425284 | lld:lifeskim |
| pubmed-article:15178680 | lifeskim:mentions | umls-concept:C0019409 | lld:lifeskim |
| pubmed-article:15178680 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:15178680 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:15178680 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15178680 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:15178680 | pubmed:dateCreated | 2004-8-9 | lld:pubmed |
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| pubmed-article:15178680 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15178680 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15178680 | pubmed:abstractText | The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy. The protein native state shows conformational heterogeneity attributable to the isomerization of the peptide bond preceding a conserved proline residue. The two equally populated cis and trans forms both adopt an elongated antiparallel three alpha-helix bundle fold but display major differences in the loop between the first two helices and at the C terminus of helix 3. Proline to alanine single point mutation of the residue Pro-30 prevents the cis/trans isomerization. The structure of the P30A mutant is similar to the structure of the trans form of AHSP in the loop 1 region. Both the wild-type AHSP and the P30A mutant bind to alpha-hemoglobin, and the wild-type conformational heterogeneity is quenched upon complex formation, suggesting that just one conformation is the active form. Changes in chemical shift observed upon complex formation identify a binding interface comprising the C terminus of helix 1, the loop 1, and the N terminus of helix 2, with the exposed residues Phe-47 and Tyr-51 being attractive targets for molecular recognition. The characteristics of this interface suggest that AHSP binds at the intradimer alpha1beta1 interface in tetrameric HbA. | lld:pubmed |
| pubmed-article:15178680 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15178680 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15178680 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15178680 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15178680 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15178680 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15178680 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15178680 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15178680 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15178680 | pubmed:author | pubmed-author:WatkinsNichol... | lld:pubmed |
| pubmed-article:15178680 | pubmed:author | pubmed-author:RutherfordTre... | lld:pubmed |
| pubmed-article:15178680 | pubmed:author | pubmed-author:BycroftMarkM | lld:pubmed |
| pubmed-article:15178680 | pubmed:author | pubmed-author:SantiveriClar... | lld:pubmed |
| pubmed-article:15178680 | pubmed:author | pubmed-author:Pérez-Cañadil... | lld:pubmed |
| pubmed-article:15178680 | pubmed:author | pubmed-author:AllenMark DMD | lld:pubmed |
| pubmed-article:15178680 | pubmed:author | pubmed-author:VadiveluMural... | lld:pubmed |
| pubmed-article:15178680 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15178680 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:15178680 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:15178680 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15178680 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15178680 | pubmed:pagination | 34963-70 | lld:pubmed |
| pubmed-article:15178680 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15178680 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15178680 | pubmed:articleTitle | NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding. | lld:pubmed |
| pubmed-article:15178680 | pubmed:affiliation | Medical Research Council Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, United Kingdom. | lld:pubmed |
| pubmed-article:15178680 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15178680 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| family:PF09236.5 | family:pubmed | pubmed-article:15178680 | lld:pfam |
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