Structural highlights
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
