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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)

  1. p120Ras-GAP binds the DLC1 Rho-GAP tumor suppressor protein and inhibits its RhoA GTPase and growth-suppressing activities. Yang XY, Guan M, Vigil D, Der CJ, Lowy DR, Popescu NC. Oncogene 28 1401-1409 (2009)
  2. Revisiting G3BP1 as a RasGAP binding protein: sensitization of tumor cells to chemotherapy by the RasGAP 317-326 sequence does not involve G3BP1. Annibaldi A, Dousse A, Martin S, Tazi J, Widmann C. PLoS One 6 e29024 (2011)
  3. Functional cross-talk between ras and rho pathways: a Ras-specific GTPase-activating protein (p120RasGAP) competitively inhibits the RhoGAP activity of deleted in liver cancer (DLC) tumor suppressor by masking the catalytic arginine finger. Jaiswal M, Dvorsky R, Amin E, Risse SL, Fansa EK, Zhang SC, Taha MS, Gauhar AR, Nakhaei-Rad S, Kordes C, Koessmeier KT, Cirstea IC, Olayioye MA, Häussinger D, Ahmadian MR. J Biol Chem 289 6839-6849 (2014)
  4. A WXW motif is required for the anticancer activity of the TAT-RasGAP317-326 peptide. Barras D, Chevalier N, Zoete V, Dempsey R, Lapouge K, Olayioye MA, Michielin O, Widmann C. J Biol Chem 289 23701-23711 (2014)
  5. Inhibition of cell migration and invasion mediated by the TAT-RasGAP317-326 peptide requires the DLC1 tumor suppressor. Barras D, Lorusso G, Rüegg C, Widmann C. Oncogene 33 5163-5172 (2014)
  6. Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions. Merő B, Radnai L, Gógl G, Tőke O, Leveles I, Koprivanacz K, Szeder B, Dülk M, Kudlik G, Vas V, Cserkaszky A, Sipeki S, Nyitray L, Vértessy BG, Buday L. J Biol Chem 294 4608-4620 (2019)


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