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Structure paper

TitleRAS interaction with Sin1 is dispensable for mTORC2 assembly and activity.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 118, Year 2021
Publish dateJan 9, 2021 (structure data deposition date)
AuthorsCastel, P. / Dharmaiah, S. / Sale, M.J. / Messing, S. / Rizzuto, G. / Cuevas-Navarro, A. / Cheng, A. / Trnka, M.J. / Urisman, A. / Esposito, D. ...Castel, P. / Dharmaiah, S. / Sale, M.J. / Messing, S. / Rizzuto, G. / Cuevas-Navarro, A. / Cheng, A. / Trnka, M.J. / Urisman, A. / Esposito, D. / Simanshu, D.K. / McCormick, F.
External linksProc. Natl. Acad. Sci. USA / PubMed:34380736
MethodsX-ray diffraction
Resolution2.35 - 2.7 Å
Structure data

PDB-7lc1:
Crystal Structure of KRAS4b (GMPPNP-bound) in complex with the RBD-PH domains of SIN1
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-7lc2:
Crystal Structure of KRAS4b-Q61R (GMPPNP-bound) in complex with the RAS-binding domain (RBD) of SIN1
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsONCOPROTEIN / Hydrolase / KRAS / RAS / K-RAS / GMPPNP / GppNHp / SIN1 / MAPKAP1 / PH DOMAIN / RBD / RAS-BINDING DOMAIN / EFFECTOR / SMALL GTPase / GppNHp MAPKAP1 / mTORC2

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