1bwy: Difference between revisions

No edit summary
No edit summary
 
Line 1: Line 1:


==NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN==
==NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN==
<StructureSection load='1bwy' size='340' side='right'caption='[[1bwy]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
<StructureSection load='1bwy' size='340' side='right'caption='[[1bwy]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bwy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWY FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bwy]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWY FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwy OCA], [https://pdbe.org/1bwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwy RCSB], [https://www.ebi.ac.uk/pdbsum/1bwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwy ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwy OCA], [https://pdbe.org/1bwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwy RCSB], [https://www.ebi.ac.uk/pdbsum/1bwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FABPH_BOVIN FABPH_BOVIN]] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.  MDGI reversibly inhibits proliferation of mammary carcinoma cells.  
[https://www.uniprot.org/uniprot/FABPH_BOVIN FABPH_BOVIN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.  MDGI reversibly inhibits proliferation of mammary carcinoma cells.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bwy ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bwy ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:7601110</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bwy" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bovin]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kveder, M]]
[[Category: Kveder M]]
[[Category: Lassen, D]]
[[Category: Lassen D]]
[[Category: Lezius, A]]
[[Category: Lezius A]]
[[Category: Luecke, C]]
[[Category: Luecke C]]
[[Category: Mesgarzadeh, A]]
[[Category: Mesgarzadeh A]]
[[Category: Rueterjans, H]]
[[Category: Rueterjans H]]
[[Category: Schmidt, J M]]
[[Category: Schmidt JM]]
[[Category: Specht, B]]
[[Category: Specht B]]
[[Category: Spener, F]]
[[Category: Spener F]]
[[Category: Fatty acid binding]]
[[Category: Fatty acid binding protein]]
[[Category: Heart muscle]]
[[Category: Intracellular lipid binding protein]]
[[Category: Lipid binding protein]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA