2eyw

From Proteopedia

(Difference between revisions)

Revision as of 15:58, 22 December 2021

N-terminal SH3 domain of CT10-Regulated Kinase

Structural highlights

2eyw is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2eyv, 2eyx, 2eyy, 2eyz
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CRK_HUMAN] 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.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

CRKI (SH2-SH3) and CRKII (SH2-SH3-SH3) are splicing isoforms of the oncoprotein CRK that regulate transcription and cytoskeletal reorganization for cell growth and motility by linking tyrosine kinases to small G proteins. CRKI shows substantial transforming activity, whereas the activity of CRKII is low, and phosphorylated CRKII has no biological activity whatsoever. The molecular mechanisms underlying the distinct biological activities of the CRK proteins remain elusive. We determined the solution structures of CRKI, CRKII and phosphorylated CRKII by NMR and identified the molecular mechanism that gives rise to their activities. Results from mutational analysis using rodent 3Y1 fibroblasts were consistent with those from the structural studies. Together, these data suggest that the linker region modulates the binding of CRKII to its targets, thus regulating cell growth and motility.

Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK.,Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F Nat Struct Mol Biol. 2007 Jun;14(6):503-10. Epub 2007 May 21. PMID:17515907^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Matsuda M, Tanaka S, Nagata S, Kojima A, Kurata T, Shibuya M. Two species of human CRK cDNA encode proteins with distinct biological activities. Mol Cell Biol. 1992 Aug;12(8):3482-9. PMID:1630456
↑ Lawrenson ID, Wimmer-Kleikamp SH, Lock P, Schoenwaelder SM, Down M, Boyd AW, Alewood PF, Lackmann M. Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling. J Cell Sci. 2002 Mar 1;115(Pt 5):1059-72. PMID:11870224
↑ Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Nat Struct Mol Biol. 2007 Jun;14(6):503-10. Epub 2007 May 21. PMID:17515907 doi:10.1038/nsmb1241
↑ Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Nat Struct Mol Biol. 2007 Jun;14(6):503-10. Epub 2007 May 21. PMID:17515907 doi:10.1038/nsmb1241

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2eyw"

@@ Line 3: / Line 3: @@
 <StructureSection load='2eyw' size='340' side='right'caption='[[2eyw]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2eyw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EYW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2eyw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EYW FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eyv|2eyv]], [[2eyx|2eyx]], [[2eyy|2eyy]], [[2eyz|2eyz]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2eyv|2eyv]], [[2eyx|2eyx]], [[2eyy|2eyy]], [[2eyz|2eyz]]</div></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=2eyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyw OCA], [http://pdbe.org/2eyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eyw RCSB], [http://www.ebi.ac.uk/pdbsum/2eyw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eyw ProSAT]</span></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=2eyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyw OCA], [https://pdbe.org/2eyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eyw RCSB], [https://www.ebi.ac.uk/pdbsum/2eyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eyw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CRK_HUMAN CRK_HUMAN]] 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.<ref>PMID:1630456</ref> <ref>PMID:11870224</ref> <ref>PMID:17515907</ref>
+[[https://www.uniprot.org/uniprot/CRK_HUMAN CRK_HUMAN]] 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.<ref>PMID:1630456</ref> <ref>PMID:11870224</ref> <ref>PMID:17515907</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 </div>
 <div class="pdbe-citations 2eyw" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Adapter molecule crk 3D structures|Adapter molecule crk 3D structures]]
 == References ==
 <references/>

2eyw

From Proteopedia

Revision as of 15:58, 22 December 2021

N-terminal SH3 domain of CT10-Regulated Kinase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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