Murine Itk SH3 domain
نویسندگان
چکیده
منابع مشابه
Proline isomerization preorganizes the Itk SH2 domain for binding to the Itk SH3 domain.
We report here the NMR-derived structure of the binary complex formed by the interleukin-2 tyrosine kinase (Itk) Src homology 3 (SH3) and Src homology 2 (SH2) domains. The interaction is independent of both a phosphotyrosine motif and a proline-rich sequence, the classical targets of the SH2 and SH3 domains, respectively. The Itk SH3/SH2 structure reveals the molecular details of this nonclassi...
متن کاملProline isomerization preorganizes the Itk SH2 domain for binding the Itk SH3 domain
We report here the NMR derived structure of the binary complex formed by the Itk SH3 and SH2 domains. The interaction is independent of both a phosphotyrosine motif and a proline-rich sequence; the classical targets of the SH2 and SH3 domain, respectively. The Itk SH3/SH2 structure reveals the molecular details of this non-classical interaction and provides a clear picture for how the previousl...
متن کاملSH3-Hunter: discovery of SH3 domain interaction sites in proteins
SH3-Hunter (http://cbm.bio.uniroma2.it/SH3-Hunter/) is a web server for the recognition of putative SH3 domain interaction sites on protein sequences. Given an input query consisting of one or more protein sequences, the server identifies peptides containing poly-proline binding motifs and associates them to a list of SH3 domains, in order to compose peptide-domain pairs. The server can accept ...
متن کاملFolding dynamics of the src SH3 domain.
The thermodynamics and kinetics of folding of the chicken src SH3 domain were characterized using equilibrium and stopped-flow fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) hydrogen exchange experiments. As found for other SH3 domains, guanidinium chloride (GdmCl) denaturation melts followed by both fluorescence and circular dichroism were nearly superimposable, in...
متن کاملMultiple folding pathways of the SH3 domain.
Experimental observations suggest that proteins follow different folding pathways under different environmental conditions. We perform molecular dynamics simulations of a model of the c-Crk SH3 domain over a broad range of temperatures, and identify distinct pathways in the folding transition. We determine the kinetic partition temperature-the temperature for which the c-Crk SH3 domain undergoe...
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ژورنال
عنوان ژورنال: Journal of Biomolecular NMR
سال: 2008
ISSN: 0925-2738,1573-5001
DOI: 10.1007/s10858-008-9231-9