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| [[Image:1bwy.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1bwy.png|left|200px]] |
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| {{STRUCTURE_1bwy| PDB=1bwy | SCENE= }} | | {{STRUCTURE_1bwy| PDB=1bwy | SCENE= }} |
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| '''NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN'''
| | ===NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN=== |
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| ==Overview==
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| The three-dimensional structure of the holo form of recombinant cellular bovine heart fatty-acid-binding protein (H-FABPc), a polypeptide of 133 amino acid residues with a molecular mass of 15 kDa, has been determined by multidimensional homonuclear and heteronuclear NMR spectroscopy applied to uniformly 15N-labeled and unlabeled protein. A nearly complete set of 1H and 15N chemical shift assignments was obtained. A total of 2329 intramolecular distance constraints and 42 side-chain chi 1 dihedral-angle constraints were derived from cross-relaxation and J coupling information. 3D nuclear Overhauser enhancement and exchange spectroscopy combined with heteronuclear multiple-quantum coherence (NOESY-HMQC) experiments, performed on a sample of uniformly 13C-labeled palmitic acid bound to unlabeled cellular heart fatty-acid-binding protein revealed 10 intermolecular contacts that determine the orientation of the bound fatty acid. An ensemble of protein conformations was calculated with the distance-geometry algorithm for NMR applications (DIANA) using the redundant dihedral-angle constraint (REDAC) strategy. After docking the fatty acid into the protein, the protein-ligand arrangement was subject to distance-restrained energy minimization. The overall conformation of the protein is a beta-barrel consisting of 10 antiparallel beta-strands which form two nearly orthogonal beta-sheets of five strands each. Two short helices form a helix-turn-helix motif in the N-terminal region of the polypeptide chain. The palmitic acid is bound within the protein in a U-shaped conformation close to the two helices. The obtained solution structure of the protein is consistent with a number of fatty-acid-binding-protein crystal structures. | | The line below this paragraph, {{ABSTRACT_PUBMED_7601110}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7601110 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7601110}} |
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| ==About this Structure== | | ==About this Structure== |
| 1BWY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWY OCA]. | | 1BWY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWY OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Heart muscle]] | | [[Category: Heart muscle]] |
| [[Category: Intracellular lipid binding protein]] | | [[Category: Intracellular lipid binding protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:03:29 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:50:47 2008'' |
