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4ykc

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Revision as of 17:04, 22 March 2017

Crystal structure of cerebral cavernous malformation 2 C-terminal adaptor domain

Structural highlights

4ykc is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	4ykd, 4yl6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CCM2_HUMAN] Hereditary cerebral cavernous malformation. The disease is caused by mutations affecting the gene represented in this entry.

Function

[CCM2_HUMAN] Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity).

Publication Abstract from PubMed

Cerebral cavernous malformation 2 (CCM2) functions as an adaptor protein implicated in various biological processes. By interacting with the mitogen-activated protein kinase MEKK3, CCM2 either mediates the activation of MEKK3 signaling in response to osmotic stress or negatively regulates MEKK3 signaling, which is important for normal cardiovascular development. However, the molecular basis governing CCM2-MEKK3 interaction is largely unknown. Here we report the crystal structure of the CCM2 C-terminal part (CCM2ct) containing both the five-helix domain (CCM2cts) and the following C-terminal tail. The end of the C-terminal tail forms an isolated helix, which interacts intramolecularly with CCM2cts. By biochemical studies we identified the N-terminal amphiphilic helix of MEKK3 (MEKK3-nhelix) as the essential structural element for CCM2ct binding. We further determined the crystal structure of CCM2cts-MEKK3-nhelix complex, in which MEKK3-nhelix binds to the same site of CCM2cts for CCM2ct intramolecular interaction. These findings build a structural framework for understanding CCM2ct-MEKK3 molecular recognition.

Structural Insights into the Molecular Recognition between Cerebral Cavernous Malformation 2 and Mitogen-Activated Protein Kinase Kinase Kinase 3.,Wang X, Hou Y, Deng K, Zhang Y, Wang DC, Ding J Structure. 2015 Apr 29. pii: S0969-2126(15)00131-8. doi:, 10.1016/j.str.2015.04.003. PMID:25982527^[1]

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

References

↑ Wang X, Hou Y, Deng K, Zhang Y, Wang DC, Ding J. Structural Insights into the Molecular Recognition between Cerebral Cavernous Malformation 2 and Mitogen-Activated Protein Kinase Kinase Kinase 3. Structure. 2015 Apr 29. pii: S0969-2126(15)00131-8. doi:, 10.1016/j.str.2015.04.003. PMID:25982527 doi:http://dx.doi.org/10.1016/j.str.2015.04.003

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ykc"

Categories: Ding, J | Wang, D C | Wang, X | Adaptor protein

@@ Line 1: / Line 1: @@
 ==Crystal structure of cerebral cavernous malformation 2 C-terminal adaptor domain==
 <StructureSection load='4ykc' size='340' side='right' caption='[[4ykc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ykd|4ykd]], [[4yl6|4yl6]]</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=4ykc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ykc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ykc RCSB], [http://www.ebi.ac.uk/pdbsum/4ykc PDBsum]</span></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=4ykc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ykc OCA], [http://pdbe.org/4ykc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ykc RCSB], [http://www.ebi.ac.uk/pdbsum/4ykc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ykc ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ykc" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4ykc

From Proteopedia

Revision as of 17:04, 22 March 2017

Crystal structure of cerebral cavernous malformation 2 C-terminal adaptor domain

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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