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| | ==Crystal structure of the CCM2 C-terminal Harmonin Homology Domain (HHD)== | | ==Crystal structure of the CCM2 C-terminal Harmonin Homology Domain (HHD)== |
| - | <StructureSection load='4fqn' size='340' side='right' caption='[[4fqn]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4fqn' size='340' side='right'caption='[[4fqn]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fqn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FQN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fqn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FQN FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C7orf22, CCM2, PP10187 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=4fqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqn OCA], [https://pdbe.org/4fqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fqn RCSB], [https://www.ebi.ac.uk/pdbsum/4fqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqn ProSAT]</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=4fqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqn OCA], [http://pdbe.org/4fqn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fqn RCSB], [http://www.ebi.ac.uk/pdbsum/4fqn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/CCM2_HUMAN CCM2_HUMAN]] Hereditary cerebral cavernous malformation. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/CCM2_HUMAN CCM2_HUMAN] Hereditary cerebral cavernous malformation. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CCM2_HUMAN 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). | + | [https://www.uniprot.org/uniprot/CCM2_HUMAN 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). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Boggon, T J]] | + | [[Category: Large Structures]] |
| - | [[Category: Fisher, O S]] | + | [[Category: Boggon TJ]] |
| - | [[Category: Li, X]] | + | [[Category: Fisher OS]] |
| - | [[Category: Murphy, J W]] | + | [[Category: Li X]] |
| - | [[Category: Zhang, R]] | + | [[Category: Murphy JW]] |
| - | [[Category: Harmonin-homology domain]]
| + | [[Category: Zhang R]] |
| - | [[Category: Helical domain]]
| + | |
| - | [[Category: Homo-dimer]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
| Structural highlights
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 malformations (CCM) are neurovascular dysplasias affecting up to 0.5% of the population. Mutations in the CCM2 gene are associated with acquisition of CCM. We identify a previously uncharacterized domain at the C-terminus of CCM2 and determine its 1.9A resolution crystal structure. Because this domain is structurally homologous to the N-terminal domain of harmonin, we name it the CCM2 harmonin-homology domain or HHD. CCM2 HHD is observed in two conformations, and we employ analytical ultracentrifugation to test its oligomerization. Additionally, CCM2 HHD contains an unusually long 13-residue 3(10) helix. This study provides the first structural characterization of CCM2. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: CCM2binds to CCM3 by pull down (View interaction) CCM2 and CCM2bind by X-ray crystallography (View interaction) CCM2 and CCM2bind by molecular sieving (View interaction).
Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus.,Fisher OS, Zhang R, Li X, Murphy JW, Demeler B, Boggon TJ FEBS Lett. 2013 Jan 31;587(3):272-7. doi: 10.1016/j.febslet.2012.12.011. Epub, 2012 Dec 22. PMID:23266514[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fisher OS, Zhang R, Li X, Murphy JW, Demeler B, Boggon TJ. Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. FEBS Lett. 2013 Jan 31;587(3):272-7. doi: 10.1016/j.febslet.2012.12.011. Epub, 2012 Dec 22. PMID:23266514 doi:http://dx.doi.org/10.1016/j.febslet.2012.12.011
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