1n8u: Difference between revisions
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==Chemosensory Protein in Complex with bromo-dodecanol== | ==Chemosensory Protein in Complex with bromo-dodecanol== | ||
<StructureSection load='1n8u' size='340' side='right' caption='[[1n8u]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1n8u' size='340' side='right' caption='[[1n8u]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BDD:BROMO-DODECANOL'>BDD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BDD:BROMO-DODECANOL'>BDD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k19|1k19]], [[1kx8|1kx8]], [[1kx9|1kx9]], [[1n8v|1n8v]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k19|1k19]], [[1kx8|1kx8]], [[1kx9|1kx9]], [[1n8v|1n8v]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8u OCA], [http://pdbe.org/1n8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n8u RCSB], [http://www.ebi.ac.uk/pdbsum/1n8u PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8u OCA], [http://pdbe.org/1n8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n8u RCSB], [http://www.ebi.ac.uk/pdbsum/1n8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n8u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<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=1n8u ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 13:09, 25 October 2017
Chemosensory Protein in Complex with bromo-dodecanolChemosensory Protein in Complex with bromo-dodecanol
Structural highlights
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 PubMedChemosensory proteins (CSPs) have been proposed to transport hydrophobic chemicals from air to olfactory or taste receptors. They have been isolated from several sensory organs of a wide range of insect species. The x-ray structure of CSPMbraA6, a 112-aa antennal protein from the moth Mamestra brassicae (Mbra), was shown to exhibit a novel type of alpha-helical fold. We have performed a structural and binding study of CSPMbraA6 to get some insights into its possible molecular function. Tryptophan fluorescence quenching demonstrates the ability of CSPMbraA6 to bind several types of semio-chemicals or surrogate ligands with microM K(d). Its crystal structure in complex with one of these compounds, 12-bromo-dodecanol, reveals extensive conformational changes on binding, resulting in the formation of a large cavity filled by three ligand molecules. Furthermore, binding cooperativity was demonstrated for some ligands, suggesting a stepwise binding. The peculiar rearrangement of CSPMbraA6 conformation and the cooperativity phenomenon might trigger the recognition of chemicals by receptors and induce subsequent signal transduction. Moth chemosensory protein exhibits drastic conformational changes and cooperativity on ligand binding.,Campanacci V, Lartigue A, Hallberg BM, Jones TA, Giudici-Orticoni MT, Tegoni M, Cambillau C Proc Natl Acad Sci U S A. 2003 Apr 29;100(9):5069-74. Epub 2003 Apr 15. PMID:12697900[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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