2YDL

Crystal structure of SH3C from CIN85

Summary for 2YDL

• Entry DOI: 10.2210/pdb2ydl/pdb
• Related: 2BZ8
• Descriptor: SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1 (2 entities in total)
• Functional Keywords: signaling protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm, cytoskeleton: Q96B97
• Total number of polymer chains: 1
• Total formula weight: 8034.96

Authors

Bravo, J.,Cardenes, N. (deposition date: 2011-03-22, release date: 2012-03-28, Last modification date: 2023-12-20)

Primary citation

Ortega Roldan, J.L.,Casares, S.,Ringkjobing Jensen, M.,Cardenes, N.,Bravo, J.,Blackledge, M.,Azuaga, A.I.,Van Nuland, N.A.J.
Distinct Ubiquitin Binding Modes Exhibited by SH3 Domains: Molecular Determinants and Functional Implications.
Plos One, 8:73018-, 2013

PubMed Abstract: SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation. We have determined the structure of the complex between first CD2AP SH3 domain and ubiquitin and performed a structural and mutational analysis to decipher the determinants of the SH3-C binding mode to ubiquitin. We found that the Phe-to-Tyr mutation in CD2AP and in the homologous CIN85 SH3-C domain does not abrogate ubiquitin binding, in contrast to previous hypothesis and our findings for the first two CD2AP SH3 domains. The similar alternative binding mode of the SH3-C domains of these related adaptor proteins is characterised by a higher affinity to C-terminal extended ubiquitin molecules. We conclude that CD2AP/CIN85 SH3-C domain interaction with ubiquitin constitutes a new ubiquitin-binding mode involved in a different cellular function and thus changes the previously established mechanism of EGF-dependent CD2AP/CIN85 mono-ubiquitination.

PubMed: 24039852
DOI: 10.1371/JOURNAL.PONE.0073018

Experimental method

X-RAY DIFFRACTION (2.05 Å)