4BXR

Structure of the wild-type TCP10 domain of Danio rerio CPAP in complex with a peptide of Danio rerio STIL

4BXR の概要

• エントリーDOI: 10.2210/pdb4bxr/pdb
• 関連するPDBエントリー: 4BXP 4BXQ
• 分子名称: CPAP, SCL-INTERRUPTING LOCUS PROTEIN HOMOLOG (3 entities in total)
• 機能のキーワード: cell cycle, centriole duplication
• 由来する生物種: DANIO RERIO (ZEBRAFISH); 詳細
• 細胞内の位置: Cytoplasm : Q8JGS1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49979.58

構造登録者

van Breugel, M. (登録日: 2013-07-15, 公開日: 2013-09-25, 最終更新日: 2023-12-20)

主引用文献

Cottee, M.A.,Muschalik, N.,Wong, Y.L.,Johnson, C.M.,Johnson, S.,Andreeva, A.,Oegema, K.,Lea, S.M.,Raff, J.W.,van Breugel, M.
Crystal structures of the CPAP/STIL complex reveal its role in centriole assembly and human microcephaly.
Elife, 2:e01071-e01071, 2013

PubMed Abstract: Centrioles organise centrosomes and template cilia and flagella. Several centriole and centrosome proteins have been linked to microcephaly (MCPH), a neuro-developmental disease associated with small brain size. CPAP (MCPH6) and STIL (MCPH7) are required for centriole assembly, but it is unclear how mutations in them lead to microcephaly. We show that the TCP domain of CPAP constitutes a novel proline recognition domain that forms a 1:1 complex with a short, highly conserved target motif in STIL. Crystal structures of this complex reveal an unusual, all-β structure adopted by the TCP domain and explain how a microcephaly mutation in CPAP compromises complex formation. Through point mutations, we demonstrate that complex formation is essential for centriole duplication in vivo. Our studies provide the first structural insight into how the malfunction of centriole proteins results in human disease and also reveal that the CPAP-STIL interaction constitutes a conserved key step in centriole biogenesis. DOI:http://dx.doi.org/10.7554/eLife.01071.001.

PubMed: 24052813
DOI: 10.7554/eLife.01071

実験手法

X-RAY DIFFRACTION (2.2 Å)