2r83: Difference between revisions

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-{{Seed}}
-[[Image:2r83.png|left|200px]]
-<!--
+==Crystal structure analysis of human synaptotagmin 1 C2A-C2B==
-The line below this paragraph, containing "STRUCTURE_2r83", creates the "Structure Box" on the page.
+<StructureSection load='2r83' size='340' side='right'caption='[[2r83]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2r83]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R83 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-{{STRUCTURE_2r83|  PDB=2r83  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r83 OCA], [https://pdbe.org/2r83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r83 RCSB], [https://www.ebi.ac.uk/pdbsum/2r83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r83 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SYT1_HUMAN SYT1_HUMAN] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
+== 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/r8/2r83_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=2r83 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Release of neurotransmitter from synaptic vesicles requires the Ca2+/phospholipid-binding protein synaptotagmin 1. There is considerable evidence that cooperation between the tandem C2 domains of synaptotagmin is a requirement of regulated exocytosis; however, high-resolution structural evidence for this interaction has been lacking. The 2.7 A crystal structure of the cytosolic domains of human synaptotagmin 1 in the absence of Ca2+ reveals a novel closed conformation of the protein. The shared interface between C2A and C2B is stabilized by a network of interactions between residues on the C-terminal alpha-helix of the C2B domain and residues on loops 1-3 of the Ca2+-binding region of C2A. These interactions alter the overall shape of the Ca2+-binding pocket of C2A, but not that of C2B. Thus, synaptotagmin 1 C2A-C2B may utilize a novel regulatory mechanism whereby one C2 domain could regulate the other until an appropriate triggering event decouples them.
-===Crystal structure analysis of human synaptotagmin 1 C2A-C2B===
+Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association.,Fuson KL, Montes M, Robert JJ, Sutton RB Biochemistry. 2007 Nov 13;46(45):13041-8. Epub 2007 Oct 23. PMID:17956130<ref>PMID:17956130</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2r83" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17956130}}, adds the Publication Abstract to the page
+*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17956130 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17956130}}
+__TOC__
+</StructureSection>
-==About this Structure==
-R83 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R83 OCA].
-==Reference==
-Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association., Fuson KL, Montes M, Robert JJ, Sutton RB, Biochemistry. 2007 Nov 13;46(45):13041-8. Epub 2007 Oct 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17956130 17956130]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Fuson, K L]]
+[[Category: Fuson KL]]
-[[Category: Montes, M.]]
+[[Category: Montes M]]
-[[Category: Robert, J J]]
+[[Category: Robert JJ]]
-[[Category: Sutton, R B.]]
+[[Category: Sutton RB]]
-[[Category: C2a-c2b]]
-[[Category: Calcium]]
-[[Category: Cell junction]]
-[[Category: Cytoplasmic vesicle]]
-[[Category: Endocytosis]]
-[[Category: Endocytosis/exocytosis complex]]
-[[Category: Exocytosis]]
-[[Category: Glycoprotein]]
-[[Category: Lipoprotein]]
-[[Category: Membrane]]
-[[Category: Metal-binding]]
-[[Category: Palmitate]]
-[[Category: Phosphorylation]]
-[[Category: Synapse]]
-[[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:30:26 2008''