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Binding, domain orientation and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases

Title data

Hofmann, Gregor ; Schweimer, Kristian ; Kiessling, Anke ; Hofinger, Edith ; Bauer, Finn ; Hoffmann, Silke ; Rösch, Paul ; Campbell, Iain D. ; Werner, Jörn M. ; Sticht, Heinrich:
Binding, domain orientation and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases.
In: Biochemistry. Vol. 44 (2005) Issue 39 . - pp. 13043-13050.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi050814y

Abstract in another language

The catalytic activity of Src-family kinases is regulated by association with its SH3 and SH2 domains. Activation requires displacement of intermolecular contacts by SH3/SH2 binding ligands resulting in dissociation of the SH3 and SH2 domains from the kinase domain. To understand the contribution of the SH3-SH2 domain pair to this regulatory process, the binding of peptides derived from physiologically relevant SH2 and SH3 interaction partners was studied for Lck and its relative Fyn by NMR spectroscopy. In contrast to Fyn, activating ligands do not induce communication between SH2 and SH3 domains in Lck. This can be attributed to the particular properties of the Lck SH3-SH2 linker which is shown to be extremely flexible thus effectively decoupling the behavior of the SH3 and SH2 domains. Measurements on the SH32 tandem from Lck further revealed a relative domain orientation that is distinctly different from that found in the Lck SH32 crystal structure and in other Src kinases. These data suggest that flexibility between SH2 and SH3 domains contributes to the adaptation of Src-family kinases to specific environments and distinct functions.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Lehrstuhl Biopolymere - Apl. Prof. Dr. Birgitta Wöhrl
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 28 Jan 2019 13:00
Last Modified: 12 Jun 2019 08:31
URI: https://eref.uni-bayreuth.de/id/eprint/47065