1bwy: Difference between revisions

Revision as of 19:50, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bwy.png

Template:STRUCTURE 1bwy

NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEINNMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN

Template:ABSTRACT PUBMED 7601110

About this StructureAbout this Structure

1BWY is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

ReferenceReference

Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy., Lassen D, Lucke C, Kveder M, Mesgarzadeh A, Schmidt JM, Specht B, Lezius A, Spener F, Ruterjans H, Eur J Biochem. 1995 May 15;230(1):266-80. PMID:7601110

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-'''NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN'''
+===NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN===
-==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}}
 ==About this Structure==
-BWY 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].
+BWY 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].
 ==Reference==
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 [[Category: Heart muscle]]
 [[Category: Intracellular lipid binding protein]]
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