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1bwy

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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'''
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===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.
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(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==
==About this Structure==
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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].
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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].
==Reference==
==Reference==
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[[Category: Heart muscle]]
[[Category: Heart muscle]]
[[Category: Intracellular lipid binding protein]]
[[Category: Intracellular lipid binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:03:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:50:47 2008''

Revision as of 16:50, 30 June 2008

Image:1bwy.png

Template:STRUCTURE 1bwy

NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN

Template:ABSTRACT PUBMED 7601110

About this Structure

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

Reference

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

Page seeded by OCA on Mon Jun 30 19:50:47 2008

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