000164352 001__ 164352
000164352 005__ 20181203022328.0
000164352 0247_ $$2doi$$a10.1016/j.molcel.2006.01.035
000164352 022__ $$a1097-2765
000164352 037__ $$aARTICLE
000164352 245__ $$aOrganization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase
000164352 269__ $$a2006
000164352 260__ $$bElsevier$$c2006
000164352 336__ $$aJournal Articles
000164352 520__ $$aThe tyrosine kinase c-Abl is inactivated by interactions made by its SH3 and SH2 domains with the distal surface of the kinase domain. We present a crystal structure of a fragment of c-Abl which reveals that a critical N-terminal cap segment, not visualized in previous structures, buttresses the SH3-SH2 substructure in the autoinhibited state and locks it onto the distal surface of the kinase domain. Surprisingly, the N-terminal cap is phosphorylated on a serine residue that interacts with the connector between the SH3 and SH2 domains. Small-angle X-ray scattering (SAXS) analysis shows that a mutated form of c-Abl, in which the N-terminal cap and two other key contacts in the autoinhibited state are deleted, exists in an extended array of the SH3, SH2, and kinase domains. This alternative conformation of Abl is likely to prolong the active state of the kinase by preventing it from returning to the autoinhibited state.
000164352 700__ $$aNagar, Bhushan
000164352 700__ $$0245280$$g209845$$aHantschel, Oliver
000164352 700__ $$aSeeliger, Markus
000164352 700__ $$aDavies, Jason M.
000164352 700__ $$aWeis, William I.
000164352 700__ $$aSuperti-Furga, Giulio
000164352 700__ $$aKuriyan, John
000164352 773__ $$j21$$tMolecular cell$$k6$$q787-98
000164352 909C0 $$xU12375$$0252328$$pUPHAN
000164352 909CO $$pSV$$particle$$ooai:infoscience.tind.io:164352
000164352 917Z8 $$x182396
000164352 937__ $$aEPFL-ARTICLE-164352
000164352 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000164352 980__ $$aARTICLE