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New page: left|200px<br /> <applet load="1hmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hmt, resolution 1.4Å" /> '''1.4 ANGSTROMS STRUCT...
 
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[[Image:1hmt.gif|left|200px]]<br />
<applet load="1hmt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hmt, resolution 1.4&Aring;" />
'''1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS'''<br />


==Overview==
==1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS==
BACKGROUND: Muscle fatty acid binding protein (M-FABP) is one of a family, of cytosolic lipid-binding proteins involved in fatty acid processing. In, order to investigate the precise interactions between M-FABP and its, ligands and to understand the structural basis of differential binding, affinity, we have compared the structures of M-FABP in complex with three, C18 fatty acids. RESULTS: We describe the crystal structures of M-FABP in, complex with n-octadecanoate (stearate), trans-delta 9-octadecenoate, (elaidate) and cis-delta 9-octadecenoate (oleate). These structures were, refined using least-squares positional and anisotropic temperature factor, refinement to final R-factors of 11.4%, 12.1% and 13.2% respectively for, all the data between 8.0 A and 1.4 A resolution. CONCLUSIONS: Stearate, elaidate and oleate each adopt highly similar U-shaped conformations when, they bind to M-FABP within a large interior binding cavity, which also, contains 13 ordered water molecules. The atomic structure of the protein, is virtually identical, regardless of the nature of the bound ligand. The, fatty acid is thought to enter the interior cavity of the protein via a, portal in its surface while interior solvent is released through a, secondary opening. The ligand affinity can be correlated with the, conformational energy and the solubility of the bound ligand.
<StructureSection load='1hmt' size='340' side='right'caption='[[1hmt]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hmt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=STE:STEARIC+ACID'>STE</scene></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=1hmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmt OCA], [https://pdbe.org/1hmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmt RCSB], [https://www.ebi.ac.uk/pdbsum/1hmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmt ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== 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/hm/1hmt_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=1hmt ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with STE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HMT OCA].
*[[Dinoflagellate luciferase|Dinoflagellate luciferase]]
 
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
==Reference==
__TOC__
Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids., Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC, Structure. 1994 Jun 15;2(6):523-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7922029 7922029]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kromminga, A.]]
[[Category: Kromminga A]]
[[Category: Patel, S.B.]]
[[Category: Patel SB]]
[[Category: Sacchettini, J.C.]]
[[Category: Sacchettini JC]]
[[Category: Scapin, G.]]
[[Category: Scapin G]]
[[Category: Veerkamp, J.H.]]
[[Category: Veerkamp JH]]
[[Category: Young, A.C.M.]]
[[Category: Young ACM]]
[[Category: STE]]
[[Category: lipid-binding protein]]
 
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Retrieved from "https://proteopedia.org/1hmt"