4FQN

Crystal structure of the CCM2 C-terminal Harmonin Homology Domain (HHD)

Summary for 4FQN

• Entry DOI: 10.2210/pdb4fqn/pdb
• Descriptor: Malcavernin (2 entities in total)
• Functional Keywords: helical domain, harmonin-homology domain, protein-protein interaction, homo-dimer, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q9BSQ5
• Total number of polymer chains: 4
• Total formula weight: 44650.40

Authors

Fisher, O.S.,Zhang, R.,Li, X.,Murphy, J.W.,Boggon, T.J. (deposition date: 2012-06-25, release date: 2012-12-19, Last modification date: 2024-02-28)

Primary citation

Fisher, O.S.,Zhang, R.,Li, X.,Murphy, J.W.,Demeler, B.,Boggon, T.J.
Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus.
Febs Lett., 587:272-277, 2013

PubMed 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.

PubMed: 23266514
DOI: 10.1016/j.febslet.2012.12.011

Experimental method

X-RAY DIFFRACTION (1.9 Å)