1IXD
Solution structure of the CAP-GLY domain from human cylindromatosis tomour-suppressor CYLD
Summary for 1IXD
| Entry DOI | 10.2210/pdb1ixd/pdb |
| Descriptor | Cylindromatosis tumour-suppressor CYLD (1 entity in total) |
| Functional Keywords | structural genomics, tumour suppressor, riken structural genomics/proteomics initiative, rsgi, antitumor protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q9NQC7 |
| Total number of polymer chains | 1 |
| Total formula weight | 10871.26 |
| Authors | Saito, K.,Koshiba, S.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-06-19, release date: 2002-12-19, Last modification date: 2023-12-27) |
| Primary citation | 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 Cited by 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: 15341735DOI: 10.1016/j.str.2004.07.012 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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