2j06 › Citations

High resolution crystal structures of the p120 RasGAP SH3 domain.

Ross B, Kristensen O, Favre D, Walicki J, Kastrup JS, Widmann C, Gajhede M
Biochem Biophys Res Commun 353 463-8 (2007)
Cited: 10 times
EuropePMC logo PMID: 17188236

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.

Articles - 2j06 mentioned but not cited (3)

  1. Lessons from high-throughput protein crystallization screening: 10 years of practical experience. Luft JR, Snell EH, Detitta GT. Expert Opin Drug Discov 6 465-480 (2011)
  2. SH3 domain regulation of RhoGAP activity: Crosstalk between p120RasGAP and DLC1 RhoGAP. Chau JE, Vish KJ, Boggon TJ, Stiegler AL. Nat Commun 13 4788 (2022)
  3. Tandem engagement of phosphotyrosines by the dual SH2 domains of p120RasGAP. Stiegler AL, Vish KJ, Boggon TJ. Structure 30 1603-1614.e5 (2022)


Reviews citing this publication (1)

  1. p120-Ras GTPase activating protein (RasGAP): a multi-interacting protein in downstream signaling. Pamonsinlapatham P, Hadj-Slimane R, Lepelletier Y, Allain B, Toccafondi M, Garbay C, Raynaud F. Biochimie 91 320-328 (2009)

Articles citing this publication (6)



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