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New page: left|200px<br /><applet load="1ckb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ckb, resolution 1.90Å" /> '''STRUCTURAL BASIS FOR...
 
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[[Image:1ckb.jpg|left|200px]]<br /><applet load="1ckb" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ckb, resolution 1.90&Aring;" />
'''STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK'''<br />


==Overview==
==STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK==
BACKGROUND: Proline-rich segments in the guanine nucleotide exchange, factor C3G bind much more strongly to the N-terminal Src homology 3 domain, (SH3-N) of the proto-oncogene product c-Crk than to other SH3 domains. The, presence of a lysine instead of an arginine in the peptides derived from, C3G appears to be crucial for this specificity towards c-Crk. RESULTS: In, order to understand the chemical basis of this specificity we have, determined the crystal structure of Crk SH3-N in complex with a high, affinity peptide from C3G (PPPALPPKKR, Kd approximately 2 microM) at 1.5 A, resolution. The peptide adopts a polyproline type II helix that binds, as, dictated by electrostatic complementarity, in reversed orientation, relative to the orientation seen in the earliest structures of SH3-peptide, complexes. A lysine in the C3G peptide is tightly coordinated by three, acidic residues in the SH3 domain. In contrast, the co-crystal structure, of c-Crk SH3-N and a peptide containing an arginine at the equivalent, position (determined at 1.9 A resolution) reveals non-optimal geometry for, the arginine and increased disorder. CONCLUSIONS: The c-Crk SH3 domain, engages in an unusual lysine-specific interaction that is rarely seen in, protein structures, and which appears to be a key determinant of its, unique ability to bind the C3G peptides with high affinity.
<StructureSection load='1ckb' size='340' side='right'caption='[[1ckb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ckb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CKB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#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=1ckb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckb OCA], [https://pdbe.org/1ckb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ckb RCSB], [https://www.ebi.ac.uk/pdbsum/1ckb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ckb 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/ck/1ckb_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=1ckb ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CKB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CKB OCA].
*[[Adapter molecule crk 3D structures|Adapter molecule crk 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk., Wu X, Knudsen B, Feller SM, Zheng J, Sali A, Cowburn D, Hanafusa H, Kuriyan J, Structure. 1995 Feb 15;3(2):215-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7735837 7735837]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Kuriyan J]]
[[Category: Kuriyan, J.]]
[[Category: Wu X]]
[[Category: Wu, X.]]
[[Category: complex (oncogene protein/peptide)]]
 
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