| pubmed-article:17954916 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17954916 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:17954916 | lifeskim:mentions | umls-concept:C0021918 | lld:lifeskim |
| pubmed-article:17954916 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:17954916 | lifeskim:mentions | umls-concept:C0086024 | lld:lifeskim |
| pubmed-article:17954916 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:17954916 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:17954916 | pubmed:issue | 44 | lld:pubmed |
| pubmed-article:17954916 | pubmed:dateCreated | 2007-11-5 | lld:pubmed |
| pubmed-article:17954916 | pubmed:abstractText | The structure of intrinsic factor (IF) in complex with cobalamin (Cbl) was determined at 2.6-A resolution. The overall fold of the molecule is that of an alpha(6)/alpha(6) barrel. It is a two-domain protein, and the Cbl is bound at the interface of the domains in a base-on conformation. Surprisingly, two full-length molecules, each comprising an alpha- and a beta-domain and one Cbl, and two truncated molecules with only an alpha- domain are present in the same asymmetric unit. The environment around Cbl is dominated by uncharged residues, and the sixth coordinate position of Co(2+) is empty. A detailed comparison between the IF-B12 complex and another Cbl transport protein complex, trans-Cbl-B12, has been made. The pH effect on the binding of Cbl analogues in transport proteins is analyzed. A possible basis for the lack of interchangeability of human and rat IF receptors is presented. | lld:pubmed |
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| pubmed-article:17954916 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17954916 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17954916 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17954916 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17954916 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17954916 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:17954916 | pubmed:author | pubmed-author:AlpersD HDH | lld:pubmed |
| pubmed-article:17954916 | pubmed:author | pubmed-author:ChefRR | lld:pubmed |
| pubmed-article:17954916 | pubmed:author | pubmed-author:MathewsF SFS | lld:pubmed |
| pubmed-article:17954916 | pubmed:author | pubmed-author:EalickS ESE | lld:pubmed |
| pubmed-article:17954916 | pubmed:author | pubmed-author:GordonM MMM | lld:pubmed |
| pubmed-article:17954916 | pubmed:author | pubmed-author:RajashankarK... | lld:pubmed |
| pubmed-article:17954916 | pubmed:author | pubmed-author:SukumarNN | lld:pubmed |
| pubmed-article:17954916 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17954916 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:17954916 | pubmed:volume | 104 | lld:pubmed |
| pubmed-article:17954916 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17954916 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17954916 | pubmed:pagination | 17311-6 | lld:pubmed |
| pubmed-article:17954916 | pubmed:dateRevised | 2010-9-15 | lld:pubmed |
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| pubmed-article:17954916 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17954916 | pubmed:articleTitle | Crystal structure of human intrinsic factor: cobalamin complex at 2.6-A resolution. | lld:pubmed |
| pubmed-article:17954916 | pubmed:affiliation | Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA. | lld:pubmed |
| pubmed-article:17954916 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17954916 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:17954916 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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