1n8v: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='1n8v' size='340' side='right'caption='[[1n8v]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n8v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cabbage_moth Cabbage moth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N8V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n8v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mamestra_brassicae Mamestra brassicae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N8V FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BDD:BROMO-DODECANOL'>BDD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.39&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n8u|1n8u]], [[1kx8|1kx8]], [[1kx9|1kx9]], [[1k19|1k19]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BDD:BROMO-DODECANOL'>BDD</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8v OCA], [http://pdbe.org/1n8v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n8v RCSB], [http://www.ebi.ac.uk/pdbsum/1n8v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n8v ProSAT]</span></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=1n8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8v OCA], [https://pdbe.org/1n8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n8v RCSB], [https://www.ebi.ac.uk/pdbsum/1n8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n8v ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9NG96_MAMBR Q9NG96_MAMBR]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 20: @@
 </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=1n8v ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Chemosensory 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<ref>PMID:12697900</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1n8v" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Cabbage moth]]
 [[Category: Large Structures]]
-[[Category: Cambillau, C]]
+[[Category: Mamestra brassicae]]
-[[Category: Campanacci, V]]
+[[Category: Cambillau C]]
-[[Category: Giudici-Orticoni, M T]]
+[[Category: Campanacci V]]
-[[Category: Hallberg, B M]]
+[[Category: Giudici-Orticoni MT]]
-[[Category: Jones, T A]]
+[[Category: Hallberg BM]]
-[[Category: Lartigue, A]]
+[[Category: Jones TA]]
-[[Category: Tegoni, M]]
+[[Category: Lartigue A]]
-[[Category: Lipid binding protein]]
+[[Category: Tegoni M]]