| pubmed-article:9655337 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9655337 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:9655337 | lifeskim:mentions | umls-concept:C0163314 | lld:lifeskim |
| pubmed-article:9655337 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9655337 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:9655337 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:9655337 | pubmed:dateCreated | 1998-9-1 | lld:pubmed |
| pubmed-article:9655337 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9655337 | pubmed:abstractText | Intestinal fatty acid-binding protein (I-FABP) is a cytosolic 15.1-kDa protein that appears to function in the intracellular transport and metabolic trafficking of fatty acids. It binds a single molecule of long-chain fatty acid in an enclosed cavity surrounded by two five-stranded antiparallel beta-sheets and a helix-turn-helix domain. To investigate the role of the helical domain, we engineered a variant of I-FABP by deleting 17 contiguous residues and inserting a Ser-Gly linker (Kim K et al., 1996, Biochemistry 35:7553-7558). This variant, termed delta17-SG, was remarkably stable, exhibited a high beta-sheet content and was able to bind fatty acids with some features characteristic of the wild-type protein. In the present study, we determined the structure of the delta17-SG/palmitate complex at atomic resolution using triple-resonance 3D NMR methods. Sequence-specific 1H, 13C, and 15N resonance assignments were established at pH 7.2 and 25 degrees C and used to define the consensus 1H/13C chemical shift-derived secondary structure. Subsequently, an iterative protocol was used to identify 2,544 NOE-derived interproton distance restraints and to calculate its tertiary structure using a unique distance geometry/simulated annealing algorithm. In spite of the sizable deletion, the delta17-SG structure exhibits a backbone conformation that is nearly superimposable with the beta-sheet domain of the wild-type protein. The selective deletion of the alpha-helical domain creates a very large opening that connects the interior ligand-binding cavity with exterior solvent. Unlike wild-type I-FABP, fatty acid dissociation from delta17-SG is structurally and kinetically unimpeded, and a protein conformational transition is not required. The delta17-SG variant of I-FABP is the only wild-type or engineered member of the intracellular lipid-binding protein family whose structure lacks alpha-helices. Thus, delta17-SG I-FABP constitutes a unique model system for investigating the role of the helical domain in ligand-protein recognition, protein stability and folding, lipid transfer mechanisms, and cellular function. | lld:pubmed |
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| pubmed-article:9655337 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9655337 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9655337 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9655337 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9655337 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9655337 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9655337 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:9655337 | pubmed:author | pubmed-author:FriedelEE | lld:pubmed |
| pubmed-article:9655337 | pubmed:author | pubmed-author:KanKK | lld:pubmed |
| pubmed-article:9655337 | pubmed:author | pubmed-author:CistolaD PDP | lld:pubmed |
| pubmed-article:9655337 | pubmed:author | pubmed-author:SteeleR ARA | lld:pubmed |
| pubmed-article:9655337 | pubmed:author | pubmed-author:HodsdonM EME | lld:pubmed |
| pubmed-article:9655337 | pubmed:author | pubmed-author:EmmertD ADA | lld:pubmed |
| pubmed-article:9655337 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9655337 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:9655337 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9655337 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9655337 | pubmed:pagination | 1332-9 | lld:pubmed |
| pubmed-article:9655337 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9655337 | pubmed:meshHeading | pubmed-meshheading:9655337-... | lld:pubmed |
| pubmed-article:9655337 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9655337 | pubmed:articleTitle | The three-dimensional structure of a helix-less variant of intestinal fatty acid-binding protein. | lld:pubmed |
| pubmed-article:9655337 | pubmed:affiliation | Department of Biochemistry & Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA. | lld:pubmed |
| pubmed-article:9655337 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9655337 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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