1IXD

Solution structure of the CAP-GLY domain from human cylindromatosis tomour-suppressor CYLD

1IXD の概要

• エントリーDOI: 10.2210/pdb1ixd/pdb
• 分子名称: Cylindromatosis tumour-suppressor CYLD (1 entity in total)
• 機能のキーワード: structural genomics, tumour suppressor, riken structural genomics/proteomics initiative, rsgi, antitumor protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q9NQC7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10871.26

構造登録者

Saito, K.,Koshiba, S.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2002-06-19, 公開日: 2002-12-19, 最終更新日: 2023-12-27)

主引用文献

Saito, K.,Kigawa, T.,Koshiba, S.,Sato, K.,Matsuo, Y.,Sakamoto, A.,Takagi, T.,Shirouzu, M.,Yabuki, T.,Nunokawa, E.,Seki, E.,Matsuda, T.,Aoki, M.,Miyata, Y.,Hirakawa, N.,Inoue, M.,Terada, T.,Nagase, T.,Kikuno, R.,Nakayama, M.,Ohara, O.,Tanaka, A.,Yokoyama, S.
The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKgamma
STRUCTURE, 12:1719-1728, 2004

PubMed Abstract: CYLD was originally identified as the human familial cylindromatosis tumor suppressor. Recently, it was reported that CYLD directly interacts with NEMO/IKKgamma and TRAF2 in the NF-kappaB signaling pathway. The two proteins bind to a region of CYLD that contains a Cys-box motif and the third cytoskeleton-associated protein-glycine conserved (CAP-Gly) domain. Here we report that the third CAP-Gly domain of CYLD specifically interacts with one of the two proline-rich sequences of NEMO/IKKgamma. The tertiary structure of the CAP-Gly domain shares the five-stranded beta sheet topology with the SH3 domain, which is well known as a proline-rich sequence-recognition domain. However, chemical shift mapping revealed that the peptide binding site of the CAP-Gly domain is formed without the long peptide binding loop characteristic of the SH3 domain. Therefore, CAP-Gly is likely to be a novel proline-rich sequence binding domain with a mechanism different from that of the SH3 domain.

PubMed: 15341735
DOI: 10.1016/j.str.2004.07.012

実験手法

SOLUTION NMR