1jjx: Difference between revisions
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==Solution Structure of Recombinant Human Brain-type Fatty acid Binding Protein== | ==Solution Structure of Recombinant Human Brain-type Fatty acid Binding Protein== | ||
<StructureSection load='1jjx' size='340' side='right' caption='[[1jjx | <StructureSection load='1jjx' size='340' side='right'caption='[[1jjx]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jjx]] is a 1 chain structure with sequence from [ | <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=' | </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'>[ | <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> | </table> | ||
== Function == | == 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 == | == 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/1jjx_consurf.spt"</scriptWhenChecked> | <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> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1jjx ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==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: Luecke | [[Category: Large Structures]] | ||
[[Category: Rademacher | [[Category: Luecke C]] | ||
[[Category: Rueterjans | [[Category: Rademacher M]] | ||
[[Category: Veerkamp | [[Category: Rueterjans H]] | ||
[[Category: Zimmerman | [[Category: Veerkamp JH]] | ||
[[Category: Zimmerman AW]] | |||
Latest revision as of 11:37, 22 May 2024
Solution Structure of Recombinant Human Brain-type Fatty acid Binding ProteinSolution Structure of Recombinant Human Brain-type Fatty acid Binding Protein
Structural highlights
FunctionFABP7_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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