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2FO0

Organization of the SH3-SH2 Unit in Active and Inactive Forms of the c-Abl Tyrosine Kinase

Summary for 2FO0
Entry DOI10.2210/pdb2fo0/pdb
DescriptorProto-oncogene tyrosine-protein kinase ABL1 (1B ISOFORM), MYRISTIC ACID, 6-(2,6-DICHLOROPHENYL)-2-{[3-(HYDROXYMETHYL)PHENYL]AMINO}-8-METHYLPYRIDO[2,3-D]PYRIMIDIN-7(8H)-ONE, ... (5 entities in total)
Functional Keywordsn-terminal cap, autoinhibition, myristoylation, sh3-sh2 clamp, phosphoserine, transferase
Biological sourceHomo sapiens (human)
More
Total number of polymer chains1
Total formula weight57292.21
Authors
Nagar, B.,Hantschel, O.,Seeliger, M.,Davies, J.M.,Weis, W.I.,Superti-Furga, G.,Kuriyan, J. (deposition date: 2006-01-12, release date: 2006-03-21, Last modification date: 2024-10-30)
Primary citationNagar, B.,Hantschel, O.,Seeliger, M.,Davies, J.M.,Weis, W.I.,Superti-Furga, G.,Kuriyan, J.
Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase.
Mol.Cell, 21:787-798, 2006
Cited by
PubMed Abstract: The 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.
PubMed: 16543148
DOI: 10.1016/j.molcel.2006.01.035
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.27 Å)
Structure validation

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数据于2024-11-06公开中

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