1g5w

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(New page: 200px<br /> <applet load="1g5w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5w" /> '''SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATT...)
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[[Image:1g5w.gif|left|200px]]<br />
 
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<applet load="1g5w" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1g5w" />
 
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'''SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN==
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Recent advances in the characterization of fatty acid-binding proteins, (FABPs) by NMR have enabled various research groups to investigate the, function of these proteins in aqueous solution. The binding of fatty acid, molecules to FABPs, which proceeds through a portal region on the protein, surface, is of particular interest. In the present study we have, determined the three-dimensional solution structure of human heart-type, FABP by multi-dimensional heteronuclear NMR spectroscopy. Subsequently, in, combination with data collected on a F57S mutant we have been able to show, that different fatty acids induce distinct conformational states of the, protein backbone in this portal region, depending on the chain length of, the fatty acid ligand. This indicates that during the binding process the, protein accommodates the ligand molecule by a "selected-fit" mechanism. In, fact, this behaviour appears to be especially pronounced in the heart-type, FABP, possibly due to a more rigid backbone structure compared with other, FABPs, as suggested by recent NMR relaxation studies. Thus differences in, the dynamic behaviours of these proteins may be the key to understanding, the variations in ligand affinity and specificity within the FABP family.
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<StructureSection load='1g5w' size='340' side='right'caption='[[1g5w]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1g5w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G5W FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5w OCA], [https://pdbe.org/1g5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g5w RCSB], [https://www.ebi.ac.uk/pdbsum/1g5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g5w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABPH_HUMAN FABPH_HUMAN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/1g5w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1g5w ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Recent advances in the characterization of fatty acid-binding proteins (FABPs) by NMR have enabled various research groups to investigate the function of these proteins in aqueous solution. The binding of fatty acid molecules to FABPs, which proceeds through a portal region on the protein surface, is of particular interest. In the present study we have determined the three-dimensional solution structure of human heart-type FABP by multi-dimensional heteronuclear NMR spectroscopy. Subsequently, in combination with data collected on a F57S mutant we have been able to show that different fatty acids induce distinct conformational states of the protein backbone in this portal region, depending on the chain length of the fatty acid ligand. This indicates that during the binding process the protein accommodates the ligand molecule by a "selected-fit" mechanism. In fact, this behaviour appears to be especially pronounced in the heart-type FABP, possibly due to a more rigid backbone structure compared with other FABPs, as suggested by recent NMR relaxation studies. Thus differences in the dynamic behaviours of these proteins may be the key to understanding the variations in ligand affinity and specificity within the FABP family.
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==About this Structure==
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Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP).,Lucke C, Rademacher M, Zimmerman AW, van Moerkerk HT, Veerkamp JH, Ruterjans H Biochem J. 2001 Mar 1;354(Pt 2):259-66. PMID:11171102<ref>PMID:11171102</ref>
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1G5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G5W OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP)., Lucke C, Rademacher M, Zimmerman AW, van Moerkerk HT, Veerkamp JH, Ruterjans H, Biochem J. 2001 Mar 1;354(Pt 2):259-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11171102 11171102]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1g5w" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Luecke, C.]]
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[[Category: Moerkerk, H.T.B.van.]]
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[[Category: Rademacher, M.]]
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[[Category: Rueterjans, H.]]
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[[Category: Veerkamp, J.H.]]
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[[Category: Zimmerman, A.]]
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[[Category: nmr spectroscopy]]
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[[Category: protein-ligand interactions]]
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[[Category: selected-fit binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:01:11 2007''
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==See Also==
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*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Luecke C]]
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[[Category: Rademacher M]]
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[[Category: Rueterjans H]]
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[[Category: Veerkamp JH]]
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[[Category: Zimmerman A]]
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[[Category: Van Moerkerk HTB]]

Current revision

SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN

PDB ID 1g5w

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