9VHM

structure of CC2D1A (coiled-coil and C2 domain containing - 1A)

Summary for 9VHM

• Entry DOI: 10.2210/pdb9vhm/pdb
• Descriptor: Coiled-coil and C2 domain-containing protein 1A (2 entities in total)
• Functional Keywords: transcriptional repressor, dna binding protein, unknown function
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 72675.89

Authors

Yeh, Y.H.,Lin, M.G.,Sun, X.H.,Hsiao, C.D. (deposition date: 2025-06-17, release date: 2026-04-29, Last modification date: 2026-06-03)

Primary citation

Yeh, Y.H.,Lin, M.G.,Sun, X.H.,Shen, Y.Y.,Ling, P.,Hsiao, C.D.
Structural characterization of the human CC2D1A fragment associated with non-syndromic intellectual disability (NSID).
Biosci.Rep., 46:-, 2026

PubMed Abstract: CC2D1A is a multidomain scaffold protein implicated in transcriptional regulation and autosomal recessive non-syndromic intellectual disability (NSID), yet its molecular mechanism is still poorly understood due to a lack of structural information. Here, we present the crystal structure of the human CC2D1A491-810 fragment, encompassing the fourth DM14 domain, a coiled-coil region, and a C-terminal C2 domain. These elements form a compact, integrated architecture, with the C2 domain mediating symmetric dimerization through conserved electrostatic interactions. In addition, a unique antiparallel β1-β10 sheet connects the coiled-coil and C2 domains, stabilizing the tertiary structure. Fluorescence polarization assays reveal micromolar DNA-binding affinity, likely mediated by the basic surface of the DM14 domain. Comparison with the Drosophila homolog Lgd highlights conserved topology with added structural features, offering insights into CC2D1A's vertebrate-specific functions and NSID-related mutations.

PubMed: 42047282
DOI: 10.1042/BSR20253955

Experimental method

X-RAY DIFFRACTION (2.3 Å)