1bwy: Difference between revisions

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New page: left|200px<br /><applet load="1bwy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bwy" /> '''NMR STUDY OF BOVINE HEART FATTY ACID BINDING...
 
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[[Image:1bwy.jpg|left|200px]]<br /><applet load="1bwy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bwy" />
'''NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN'''<br />


==Overview==
==NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN==
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.
<StructureSection load='1bwy' size='340' side='right'caption='[[1bwy]]' scene=''>
== Structural highlights ==
<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='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>
== 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bw/1bwy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


==About this Structure==
==See Also==
1BWY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BWY OCA].
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7601110 7601110]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[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]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:58:56 2007''

Latest revision as of 18:36, 13 March 2024

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

Structural highlights

1bwy is a 1 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

Drag the structure with the mouse to rotate

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