4uy2: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
 ==Crystal structure of the complex of the extracellular domain of human alpha9 nAChR with alpha-bungarotoxin.==
-<StructureSection load='4uy2' size='340' side='right' caption='[[4uy2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='4uy2' size='340' side='right'caption='[[4uy2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4uy2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UY2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4uy2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UY2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.697&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uxu|4uxu]], [[4d01|4d01]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4uy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uy2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uy2 RCSB], [http://www.ebi.ac.uk/pdbsum/4uy2 PDBsum]</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=4uy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uy2 OCA], [https://pdbe.org/4uy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uy2 RCSB], [https://www.ebi.ac.uk/pdbsum/4uy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uy2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACHA9_HUMAN ACHA9_HUMAN]] Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding may induce an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane. In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. May also regulate keratinocyte adhesion.<ref>PMID:11752216</ref> <ref>PMID:11021840</ref>  [[http://www.uniprot.org/uniprot/NXL1V_BUNMU NXL1V_BUNMU]] Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to muscular and neuronal (alpha-7, alpha-8, and alpha-9) nicotinic acetylcholine receptors.
+[https://www.uniprot.org/uniprot/ACHA9_HUMAN ACHA9_HUMAN] Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding may induce an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane. In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. May also regulate keratinocyte adhesion.<ref>PMID:11752216</ref> <ref>PMID:11021840</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4uy2" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
+*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
 == References ==
 <references/>
@@ Line 22: / Line 28: @@
 </StructureSection>
 [[Category: Bungarus multicinctus]]
-[[Category: Giastas, P]]
+[[Category: Homo sapiens]]
-[[Category: Tzartos, S J]]
+[[Category: Large Structures]]
-[[Category: Zarkadas, E]]
+[[Category: Giastas P]]
-[[Category: Zouridakis, M]]
+[[Category: Tzartos SJ]]
-[[Category: Cys-loop receptor]]
+[[Category: Zarkadas E]]
-[[Category: Ligand binding domain]]
+[[Category: Zouridakis M]]
-[[Category: Toxin-binding protein-toxin complex]]