PUBLICATION

Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture

Authors
Hatzopoulos, G.N., Erat, M.C., Cutts, E., Rogala, K.B., Slater, L.M., Stansfeld, P.J., Vakonakis, I.
ID
ZDB-PUB-200522-23
Date
2013
Source
Structure (London, England : 1993)   21: 2069-77 (Journal)
Registered Authors
Keywords
none
MeSH Terms
  • Animals
  • Cell Cycle Proteins
  • Centrioles/chemistry*
  • Crystallography, X-Ray
  • Humans
  • Microcephaly/genetics
  • Microtubule-Associated Proteins/chemistry*
  • Microtubule-Associated Proteins/genetics
  • Models, Molecular
  • Mutation, Missense
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Zebrafish*
  • Zebrafish Proteins/chemistry*
  • Zebrafish Proteins/genetics
PubMed
24076405 Full text @ Structure
Abstract
Centrioles are evolutionarily conserved eukaryotic organelles composed of a protein scaffold surrounded by sets of microtubules organized with a 9-fold radial symmetry. CPAP, a centriolar protein essential for microtubule recruitment, features a C-terminal domain of unknown structure, the G-box. A missense mutation in the G-box reduces affinity for the centriolar shuttling protein STIL and causes primary microcephaly. Here, we characterize the molecular architecture of CPAP and determine the G-box structure alone and in complex with a STIL fragment. The G-box comprises a single elongated β sheet capable of forming supramolecular assemblies. Structural and biophysical studies highlight the conserved nature of the CPAP-STIL complex. We propose that CPAP acts as a horizontal "strut" that joins the centriolar scaffold with microtubules, whereas G-box domains form perpendicular connections.
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