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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKgamma.

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.[1]

References

  1. The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKgamma. 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. Structure (Camb.) (2004) [Pubmed]
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