1jjj: Difference between revisions
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==SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN== | ==SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN== | ||
<StructureSection load='1jjj' size='340' side='right' caption='[[1jjj | <StructureSection load='1jjj' size='340' side='right'caption='[[1jjj]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jjj]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1jjj]] 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=1JJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JJJ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1jjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjj OCA], [https://pdbe.org/1jjj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jjj RCSB], [https://www.ebi.ac.uk/pdbsum/1jjj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjj ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FABP5_HUMAN FABP5_HUMAN] High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/1jjj_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/1jjj_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1jjj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Fatty acid-binding protein|Fatty acid-binding protein]] | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Gutierrez-Gonzalez | [[Category: Large Structures]] | ||
[[Category: Hanhoff | [[Category: Gutierrez-Gonzalez LH]] | ||
[[Category: Hohoff | [[Category: Hanhoff T]] | ||
[[Category: Ludwig | [[Category: Hohoff C]] | ||
[[Category: Luecke | [[Category: Ludwig C]] | ||
[[Category: Rademacher | [[Category: Luecke C]] | ||
[[Category: Rueterjans | [[Category: Rademacher M]] | ||
[[Category: Spener | [[Category: Rueterjans H]] | ||
[[Category: Spener F]] | |||
Latest revision as of 11:33, 6 November 2024
SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEINSOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN
Structural highlights
FunctionFABP5_HUMAN High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman epidermal-type fatty acid-binding protein (E-FABP) belongs to a family of intracellular 14-15 kDa lipid-binding proteins, whose functions have been associated with fatty acid signalling, cell growth, regulation and differentiation. As a contribution to understanding the structure-function relationship, we report in the present study features of its solution structure and backbone dynamics determined by NMR spectroscopy. Applying multi-dimensional high-resolution NMR techniques on unlabelled and 15N-enriched recombinant human E-FABP, the 1H and 15N resonance assignments were completed. On the basis of 2008 distance restraints, the three-dimensional solution structure of human E-FABP was subsequently obtained (backbone atom root-mean-square deviation of 0.92+/-0.11 A; where 1 A=0.1 nm), consisting mainly of 10 anti-parallel beta-strands that form a beta-barrel structure. 15N relaxation experiments (T1, T2 and heteronuclear nuclear Overhauser effects) at 500, 600 and 800 MHz provided information on the internal dynamics of the protein backbone. Nearly all non-terminal backbone amide groups showed order parameters S(2)>0.8, with an average value of 0.88+/-0.04, suggesting a uniformly low backbone mobility in the nanosecond-to-picosecond time range. Moreover, hydrogen/deuterium exchange experiments indicated a direct correlation between the stability of the hydrogen-bonding network in the beta-sheet structure and the conformational exchange in the millisecond-to-microsecond time range. The features of E-FABP backbone dynamics elaborated in the present study differ markedly from those of the phylogenetically closely related heart-type FABP and the more distantly related ileal lipid-binding protein, implying a strong interdependence with the overall protein stability and possibly also with the ligand-binding affinity for members of the lipid-binding protein family. Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP).,Gutierrez-Gonzalez LH, Ludwig C, Hohoff C, Rademacher M, Hanhoff T, Ruterjans H, Spener F, Lucke C Biochem J. 2002 Jun 15;364(Pt 3):725-37. PMID:12049637[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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