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FEBS Lett. 2013 Jan 31;587(3):272-7. doi: 10.1016/j.febslet.2012.12.011. Epub 2012 Dec 22.

Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus.

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1
Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.

Abstract

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 1.9Å 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.

PMID:
23266514
PMCID:
PMC3558538
DOI:
10.1016/j.febslet.2012.12.011
[Indexed for MEDLINE]
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