Murine Itk SH3 domain

dc.contributor.author Andreotti, Amy
dc.contributor.author Fulton, D. Bruce
dc.contributor.author Severin, Andrew
dc.contributor.department Biochemistry, Biophysics and Molecular Biology
dc.date 2018-02-20T16:34:09.000
dc.date.accessioned 2020-06-29T23:46:16Z
dc.date.available 2020-06-29T23:46:16Z
dc.date.copyright Tue Jan 01 00:00:00 UTC 2008
dc.date.issued 2008-04-01
dc.description.abstract <p>Interleukin-2 tyrosine kinase (Itk) is a non-receptor tyrosine kinase of the Tec family that is activated upon antigen binding to the T cell receptor (Schwartzberg et al. 2005; Berg 2007). Itk is comprised of four regulatory domains: PH (Pleckstrin homology), TH (Tec homology), SH3, SH2 and the catalytic kinase domain. SH3 domains share a common fold consisting of five anti-parallel β strands that form a β barrel and bind canonical proline rich ligands as well as a variety of noncanonical ligands (Agrawal and Kishan 2002).</p>
dc.description.comments <p>This is a post-peer-review, pre-copyedit version of an article published in Journal of Biomolecular NMR. The final authenticated version is available online at: <a href="http://dx.doi.org/10.1117/12.911289" target="_blank">http://dx.doi.org/10.1007/s10858-008-9231-9</a>.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/bbmb_ag_pubs/185/
dc.identifier.articleid 1201
dc.identifier.contextkey 11597486
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath bbmb_ag_pubs/185
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/10649
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/bbmb_ag_pubs/185/2008_Andreotti_MurineDomainManuscript.pdf|||Fri Jan 14 21:43:02 UTC 2022
dc.source.uri 10.1007/s10858-008-9231-9
dc.subject.disciplines Biochemistry
dc.subject.disciplines Biophysics
dc.subject.disciplines Molecular Biology
dc.subject.disciplines Structural Biology
dc.title Murine Itk SH3 domain
dc.type article
dc.type.genre article
dspace.entity.type Publication
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relation.isAuthorOfPublication 87268d62-4b33-4949-a936-2d6d1ff1cfe2
relation.isOrgUnitOfPublication c70f85ae-e0cd-4dce-96b5-4388aac08b3f
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