4LD3

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

4LD3 の概要

• エントリーDOI: 10.2210/pdb4ld3/pdb
• 関連するPDBエントリー: 4LD1 4lzf
• 分子名称: Uncharacterized protein, SCL-interrupting locus protein homolog, ISOPROPYL ALCOHOL, ... (5 entities in total)
• 機能のキーワード: g-box, beta-sheet, centriole organisation, structural protein, protein binding
• 由来する生物種: Danio rerio (leopard danio,zebra danio,zebra fish); 詳細
• 細胞内の位置: Cytoplasm (Potential): Q8JGS1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27663.90

構造登録者

Hatzopoulos, G.N.,Vakonakis, I. (登録日: 2013-06-24, 公開日: 2013-09-04, 最終更新日: 2024-02-28)

主引用文献

Hatzopoulos, G.N.,Erat, M.C.,Cutts, E.,Rogala, K.B.,Slater, L.M.,Stansfeld, P.J.,Vakonakis, I.
Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture.
Structure, 21:2069-2077, 2013

PubMed 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.

PubMed: 24076405
DOI: 10.1016/j.str.2013.08.019

実験手法

X-RAY DIFFRACTION (2.44 Å)