4fqn
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[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). | [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;"> | ||
| - | == 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). | ||
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| - | 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<ref>PMID:23266514</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4fqn" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of the CCM2 C-terminal Harmonin Homology Domain (HHD)
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Categories: Homo sapiens | Large Structures | Boggon TJ | Fisher OS | Li X | Murphy JW | Zhang R
