ArticleProtein science : a publication of the Protein Society2006
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.International reviews in physical chemistry · 2013Article
- Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 2. Exchange kinetics.Molecular pharmaceutics · 2012Article
- The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.Protein science : a publication of the Protein Society · 2007Article
- Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein.Journal of molecular biology · 2007Article
- Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis.Journal of the American Society for Mass Spectrometry · 2006Article
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Authors and funding
4 authors.
Funding
Abstract
The Tip protein from Herpesvirus saimiri interacts with the SH3 domain from the Src-family kinase Lck via a proline-containing sequence termed LBD1. Src-family kinase SH3 domains related to Lck have been shown to be dynamic in solution and partially unfold under physiological conditions. The rate of such partial unfolding is reduced by viral protein binding. To determine if the Lck SH3 domain displayed similar behavior, the domain was investigated with hydrogen exchange and mass spectrometry. Lck SH3 was found to be highly dynamic in solution. While other SH3 domains require as much as 10,000 sec to become totally deuterated, Lck SH3 became almost completely labeled within 200 sec. A partial unfolding event involving 8-10 residues was observed with a half-life of approximately 10 sec. Tip LBD1 binding did not cause gross structural changes in Lck SH3 but globally stabilized the domain and reduced the rate of partial unfolding by a factor of five. The region of partial unfolding in Lck SH3 was found to be similar to that identified for other SH3 domains that partially unfold. Although the sequence conservation between Lck SH3 and other closely related SH3 domains is high, the dynamics do not appear to be conserved.
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