4ld3 | pdb_00004ld3

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

spinqualitylabelsall models 4ld3, resolution 2.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ld3 is a 2 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, IPA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E7FCY1_DANRE Publication Abstract from PubMed 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 beta 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. Structural Analysis of the G-Box Domain of the Microcephaly Protein CPAP Suggests a Role in Centriole Architecture.,Hatzopoulos GN, Erat MC, Cutts E, Rogala KB, Slater LM, Stansfeld PJ, Vakonakis I Structure. 2013 Sep 24. pii: S0969-2126(13)00340-7. doi:, 10.1016/j.str.2013.08.019. PMID:24076405 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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