1m3c: Difference between revisions

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New page: left|200px<br /><applet load="1m3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3c" /> '''Solution structure of a circular form of the...
 
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[[Image:1m3c.jpg|left|200px]]<br /><applet load="1m3c" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m3c" />
'''Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G mutant) from oncogene protein c-Crk'''<br />


==About this Structure==
==Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G mutant) from oncogene protein c-Crk==
1M3C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M3C OCA].  
<StructureSection load='1m3c' size='340' side='right'caption='[[1m3c]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M3C FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1m3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m3c OCA], [https://pdbe.org/1m3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m3c RCSB], [https://www.ebi.ac.uk/pdbsum/1m3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m3c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CRK_MOUSE CRK_MOUSE] The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.
== 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/m3/1m3c_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1m3c ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Adapter molecule crk 3D structures|Adapter molecule crk 3D structures]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Camarero JA]]
[[Category: Camarero, J.A.]]
[[Category: Fushman D]]
[[Category: Fushman, D.]]
[[Category: Hall JB]]
[[Category: Hall, J.B.]]
[[Category: Schumann FH]]
[[Category: Schumann, F.H.]]
[[Category: Tayakuniyil PP]]
[[Category: Tayakuniyil, P.P.]]
[[Category: Varadan R]]
[[Category: Varadan, R.]]
[[Category: adaptor protein]]
[[Category: circular protein]]
[[Category: cyclized protein]]
[[Category: sh3]]
[[Category: sh3 domain]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:06:54 2007''

Latest revision as of 08:37, 6 November 2024

Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G mutant) from oncogene protein c-Crk

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