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1. Characterization of Lck-binding elements in the herpesviral regulatory tip protein

Author

Bauer, Finn, Hofinger, Edith, Hoffman, Silke, Rosch, Paul, Schweimer, Kristian, and Heinrich, Sticht

Subjects
Hydrophobic effect -- Observations, Nuclear magnetic resonance spectroscopy -- Research, Tyrosine -- Research, Biological sciences, Chemistry
Abstract

The interaction of tyrosine kinase interacting protein (Tip) with the regulatory SH3 and SH2 domains of Lck was investigated by biophysical and computational techniques. The existence of numerous interaction sites between Tip and the regulatory domains of Lck implies a complex regulatory mechanism and may have evolved to allow a gradual regulation of Lck activity in different pathogenic states.

Published
2004

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