| pubmed-article:2682622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2682622 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:2682622 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:2682622 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:2682622 | lifeskim:mentions | umls-concept:C0003601 | lld:lifeskim |
| pubmed-article:2682622 | lifeskim:mentions | umls-concept:C0163314 | lld:lifeskim |
| pubmed-article:2682622 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2682622 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:2682622 | pubmed:dateCreated | 1989-12-1 | lld:pubmed |
| pubmed-article:2682622 | pubmed:abstractText | Rat intestinal fatty acid binding protein (I-FABP) is a member of a family of cytoplasmic hydrophobic ligand-binding proteins. To gain insights about the contribution of bound fatty acid to I-FABP's conformation and mechanism of ligand binding, we have determined the structure of Escherichia coli-derived rat apo-I-FABP to 1.96-A resolution and compared it to the recently refined structure of I-FABP with bound palmitate. Both apo- and holo-I-FABP are composed primarily of anti-parallel beta-strands which form two nearly orthogonal beta-sheets ("beta-clam"). The overall structures of the apo- and holo-I-FABP are nearly identical, with a root mean square (rms) difference of 0.37 A between C alpha atoms, 0.38 A between all main-chain atoms, and 0.94 A between all side-chain atoms. However, rms differences of greater than 1.3 A were noted for the side chains of Ile-23, Lys-27, Arg-56, Leu-72, Ala-73, and Asp-74. The space occupied by bound ligand in the core of the holoprotein is occupied in the apo-protein by ordered solvent molecules. This results in an increase in the total number of internal ordered solvent molecules from 7 in the holoprotein to 13 in apo-I-FABP. This finding, together with observed differences in the side-chain orientations of two residues (Arg-56 and Lys-27) situated over a potential opening to the cores of the apo- and holoproteins, suggests that solvent molecules play a critical role in ligand binding. Moreover, the data indicate that the beta-clam structure is stable even in the absence of bound ligand. | lld:pubmed |
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| pubmed-article:2682622 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2682622 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2682622 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2682622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2682622 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2682622 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2682622 | pubmed:author | pubmed-author:GordonJ IJI | lld:pubmed |
| pubmed-article:2682622 | pubmed:author | pubmed-author:BanaszakL JLJ | lld:pubmed |
| pubmed-article:2682622 | pubmed:author | pubmed-author:SacchettiniJ... | lld:pubmed |
| pubmed-article:2682622 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2682622 | pubmed:volume | 86 | lld:pubmed |
| pubmed-article:2682622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2682622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2682622 | pubmed:pagination | 7736-40 | lld:pubmed |
| pubmed-article:2682622 | pubmed:dateRevised | 2010-9-9 | lld:pubmed |
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| pubmed-article:2682622 | pubmed:meshHeading | pubmed-meshheading:2682622-... | lld:pubmed |
| pubmed-article:2682622 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2682622 | pubmed:articleTitle | Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli. | lld:pubmed |
| pubmed-article:2682622 | pubmed:affiliation | Department of Biochemistry, Washington University School of Medicine, Saint Louis, MO 63110. | lld:pubmed |
| pubmed-article:2682622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2682622 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2682622 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:25598 | entrezgene:pubmed | pubmed-article:2682622 | lld:entrezgene |
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