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New page: left|200px<br /> <applet load="1jjx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jjx" /> '''Solution Structure of Recombinant Human Bra...
 
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[[Image:1jjx.gif|left|200px]]<br />
<applet load="1jjx" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jjx" />
'''Solution Structure of Recombinant Human Brain-type Fatty acid Binding Protein'''<br />


==Overview==
==Solution Structure of Recombinant Human Brain-type Fatty acid Binding Protein==
Human brain-type fatty acid-binding protein (B-FABP) has been, recombinantly expressed in Escherichia coli both unlabelled and, 15N-enriched for structure investigation in solution using high-resolution, NMR spectroscopy. The sequential assignments of the 1H and 15N resonances, were achieved by applying multidimensional homo- and heteronuclear NMR, experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a, total of 2490 meaningful distance constraints. The overall B-FABP, structure exhibits the typical backbone conformation described for other, members of the FABP family, consisting often antiparallel beta-strands, (betaA to betaJ) that form two almost orthogonal beta-sheets, a, helix-turn-helix motif that closes the beta-barrel on one side, and a, short N-terminal helical loop. A comparison with the crystal structure of, the same protein complexed with docosahexaenoic acid reveals only minor, differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP, and heart-type FABP with respect to fatty acid binding inside the protein, cavity.
<StructureSection load='1jjx' size='340' side='right'caption='[[1jjx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jjx]] 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=1JJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JJX 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=1jjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjx OCA], [https://pdbe.org/1jjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jjx RCSB], [https://www.ebi.ac.uk/pdbsum/1jjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABP7_HUMAN FABP7_HUMAN] B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (By similarity).
== 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/jj/1jjx_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=1jjx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and 15N-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the 1H and 15N resonances were achieved by applying multidimensional homo- and heteronuclear NMR experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a total of 2490 meaningful distance constraints. The overall B-FABP structure exhibits the typical backbone conformation described for other members of the FABP family, consisting often antiparallel beta-strands (betaA to betaJ) that form two almost orthogonal beta-sheets, a helix-turn-helix motif that closes the beta-barrel on one side, and a short N-terminal helical loop. A comparison with the crystal structure of the same protein complexed with docosahexaenoic acid reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity.


==Disease==
Solution structure of fatty acid-binding protein from human brain.,Rademacher M, Zimmerman AW, Ruterjans H, Veerkamp JH, Lucke C Mol Cell Biochem. 2002 Oct;239(1-2):61-8. PMID:12479569<ref>PMID:12479569</ref>
Known diseases associated with this structure: Infundibular hypoplasia and hypopituitarism OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=313430 313430]], Mental retardation, X-linked, with isolated growth hormone deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=313430 313430]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1JJX 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=1JJX OCA].
</div>
<div class="pdbe-citations 1jjx" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Solution structure of fatty acid-binding protein from human brain., Rademacher M, Zimmerman AW, Ruterjans H, Veerkamp JH, Lucke C, Mol Cell Biochem. 2002 Oct;239(1-2):61-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12479569 12479569]
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Luecke, C.]]
[[Category: Luecke C]]
[[Category: Rademacher, M.]]
[[Category: Rademacher M]]
[[Category: Rueterjans, H.]]
[[Category: Rueterjans H]]
[[Category: Veerkamp, J.H.]]
[[Category: Veerkamp JH]]
[[Category: Zimmerman, A.W.]]
[[Category: Zimmerman AW]]
[[Category: 15n isotope enrichment]]
[[Category: beta barrel]]
[[Category: fatty acid carrier]]
[[Category: lipid binding protein]]
[[Category: nmr spectroscopy]]
 
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