1mdy: 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 MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION==
-<StructureSection load='1mdy' size='340' side='right' caption='[[1mdy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='1mdy' size='340' side='right'caption='[[1mdy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mdy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MDY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mdy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MDY 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=1mdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mdy OCA], [http://pdbe.org/1mdy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mdy RCSB], [http://www.ebi.ac.uk/pdbsum/1mdy 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]] 2.8&#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=1mdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mdy OCA], [https://pdbe.org/1mdy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mdy RCSB], [https://www.ebi.ac.uk/pdbsum/1mdy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mdy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYOD1_MOUSE MYOD1_MOUSE]] Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Activates muscle-specific promoters. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins.<ref>PMID:3175662</ref>
+[https://www.uniprot.org/uniprot/MYOD1_MOUSE MYOD1_MOUSE] Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Activates muscle-specific promoters. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins.<ref>PMID:3175662</ref>
 == 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/md/1mdy_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/md/1mdy_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=1mdy ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA complex has been solved and refined at 2.8 A resolution. This structure proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are remarkably similar; it helps us understand subtle differences in binding preferences for these proteins; and it has surprising implications for our understanding of transcription. Specifically, Ala-114 and Thr-115, which are required for positive control in the myogenic proteins, are buried at the protein-DNA interface. These residues are not available for direct protein-protein contacts, but they may determine the conformation of Arg-111. Comparisons with Max suggest that the conformation of this arginine, which is different in the two structures, may play an important role in myogenic transcription.
-Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation.,Ma PC, Rould MA, Weintraub H, Pabo CO Cell. 1994 May 6;77(3):451-9. PMID:8181063<ref>PMID:8181063</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mdy" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[User:John S. de Banzie/DNA-BindingHelixLoopHelix|User:John S. de Banzie/DNA-BindingHelixLoopHelix]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Ma, P C.M]]
+[[Category: Ma PCM]]
-[[Category: Pabo, C O]]
+[[Category: Pabo CO]]
-[[Category: Rould, M A]]
+[[Category: Rould MA]]
-[[Category: Weintraub, H]]
+[[Category: Weintraub H]]
-[[Category: Protein-dna complex]]
-[[Category: Transcription-dna complex]]