2J05

Crystal structure of the RasGAP SH3 domain at 1.5 Angstrom resolution

Summary for 2J05

• Entry DOI: 10.2210/pdb2j05/pdb
• Related: 1WER 1WQ1 2J06
• Descriptor: RAS GTPASE-ACTIVATING PROTEIN 1 (2 entities in total)
• Functional Keywords: gtpase activation, sh3 domain, sh2 domain, src homology 3, ras signaling pathway, gtpase activating protein, proto-oncogene, phosphorylation, disease mutation, signal transduction
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: P20936
• Total number of polymer chains: 2
• Total formula weight: 15530.67

Authors

Ross, B.,Gajhede, M.,Kristensen, O. (deposition date: 2006-08-01, release date: 2007-01-02, Last modification date: 2024-11-13)

Primary citation

Ross, B.,Kristensen, O.,Favre, D.,Walicki, J.,Kastrup, J.S.,Widmann, C.,Gajhede, M.
High Resolution Crystal Structures of the P120 Rasgap SH3 Domain.
Biochem.Biophys.Res.Commun., 353:463-, 2007

PubMed Abstract: X-ray structures of two crystal forms of the Src homology 3 domain (SH3) of the Ras GTPase activating protein (RasGAP) were determined at 1.5 and 1.8A resolution. The overall structure comprises a single domain with two tightly packed beta-sheets linked by a short helical segment. An important motif for peptide binding in other SH3 domains is not conserved in RasGAP. The RasGAP SH3 domain forms dimers in the crystal structures, which may provide new functional insight. The dimer interface involves residues also present in a peptide previously identified as an apoptotic sensitizer of tumor cells.

PubMed: 17188236
DOI: 10.1016/J.BBRC.2006.12.044

Experimental method

X-RAY DIFFRACTION (1.5 Å)