1dsl: Difference between revisions

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

OCA

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 ==GAMMA B CRYSTALLIN C-TERMINAL DOMAIN==
-<StructureSection load='1dsl' size='340' side='right' caption='[[1dsl]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='1dsl' size='340' side='right'caption='[[1dsl]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dsl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DSL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dsl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DSL FirstGlance]. <br>
-</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=1dsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsl OCA], [http://pdbe.org/1dsl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dsl RCSB], [http://www.ebi.ac.uk/pdbsum/1dsl PDBsum]</span></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]] 1.55&#8491;</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=1dsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsl OCA], [https://pdbe.org/1dsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dsl RCSB], [https://www.ebi.ac.uk/pdbsum/1dsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dsl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CRGB_BOVIN CRGB_BOVIN]] Crystallins are the dominant structural components of the vertebrate eye lens.
+[https://www.uniprot.org/uniprot/CRGB_BOVIN CRGB_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens.
 == 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/ds/1dsl_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/1dsl_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1dsl ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of gamma beta-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in beta gamma-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice.
-The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins.,Norledge BV, Mayr EM, Glockshuber R, Bateman OA, Slingsby C, Jaenicke R, Driessen HP Nat Struct Biol. 1996 Mar;3(3):267-74. PMID:8605629<ref>PMID:8605629</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Crystallin 3D structures|Crystallin 3D structures]]
-<div class="pdbe-citations 1dsl" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Bos taurus]]
-[[Category: Bateman, O A]]
+[[Category: Large Structures]]
-[[Category: Driessen, H P.C]]
+[[Category: Bateman OA]]
-[[Category: Glockshuber, R]]
+[[Category: Driessen HPC]]
-[[Category: Jaenicke, R]]
+[[Category: Glockshuber R]]
-[[Category: Mayr, E M]]
+[[Category: Jaenicke R]]
-[[Category: Norledge, B V]]
+[[Category: Mayr E-M]]
-[[Category: Slingsby, C]]
+[[Category: Norledge BV]]
-[[Category: Eye lens protein]]
+[[Category: Slingsby C]]
-[[Category: Multigene family]]