4LZF
A novel domain in the microcephaly protein CPAP suggests a role in centriole architecture
4LZF の概要
| エントリーDOI | 10.2210/pdb4lzf/pdb |
| 関連するPDBエントリー | 4LD1 4LD3 |
| 分子名称 | Centrosomal P4.1-associated protein, SCL-interrupting locus protein homolog, TRIETHYLENE GLYCOL, ... (6 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 : Q8JGS1 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 23070.85 |
| 構造登録者 | Hatzopoulos, G.N.,Erat, M.C.,Cutts, E.,Rogala, K.,Slatter, L.,Stansfeld, P.J.,Vakonakis, I. (登録日: 2013-07-31, 公開日: 2013-09-11, 最終更新日: 2023-09-20) |
| 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 Cited by 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: 24076405DOI: 10.1016/j.str.2013.08.019 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.72 Å) |
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