Motion in c-Src tyrosine kinase [csrc]

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Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures 1FMK Conformation 1 [ PartsList ] 2SRC Conformation 2

Description Structure of a large fragment of the c-Src tyrosine kinase shows that interactions among domains, stabilized by binding of the phosphorylated tail to the SH2 domain, lock the molecule in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. N lobe rotates 9 degress relative to its position in the cAPK Sidechain of Glu310 moves 12 A.

Particular values describing motion Maximum CA displacement (A) = 12 (from lit.) Maximum Rotation (degrees) = 9 (from lit.) Experimental Methods = x (Traditional x-ray) Creation Date = 19970822 Modification Date = 19971212

References Xu W, Harrison SC, Eck MJ (1997). Three-dimensional structure of the tyrosine kinase c-Src. 385(6617):595-602 [Medline info for 97177105]

Data and Graphics Graphic-1 Overall motion

GO terms associated with structures Molecular function ATP binding, protein kinase activity, protein-tyrosine kinase activity Biological process protein amino acid phosphorylation, intracellular signaling cascade

Morphs

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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu