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000049408 0247_ $$2DOI$$a10.1021/bi050814y
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000049408 041__ $$aeng
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000049408 084__ $$2WoS$$aBiochemistry & Molecular Biology
000049408 1001_ $$0P:(DE-HGF)0$$aHofmann, G.$$b0
000049408 245__ $$aBinding, domain orientation, and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases
000049408 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2005
000049408 300__ $$a13043 - 13050
000049408 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000049408 440_0 $$0798$$aBiochemistry$$v44$$x0006-2960$$y39
000049408 500__ $$aRecord converted from VDB: 12.11.2012
000049408 520__ $$aThe catalytic activity of Src-family kinases is regulated by association with its SH3 and SH2 domains. Activation requires displacement of intermolecular contacts by SH3/SH2 binding ligands resulting in dissociation of the SH3 and SH2 domains from the kinase domain. To understand the contribution of the SH3-SH2 domain pair to this regulatory process, the binding of peptides derived from physiologically relevant SH2 and SH3 interaction partners was studied for Lck and its relative Fyn by NMR spectroscopy. In contrast to Fyn, activating ligands do not induce communication between SH2 and SH3 domains in Lck. This can be attributed to the particular properties of the Lck SH3-SH2 linker which is shown to be extremely flexible thus effectively decoupling the behavior of the SH3 and SH2 domains. Measurements on the SH32 tandem from Lck further revealed a relative domain orientation that is distinctly different from that found in the Lck SH32 crystal structure and in other Src kinases. These data suggest that flexibility between SH2 and SH3 domains contributes to the adaptation of Src-family kinases to specific environments and distinct functions.
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000049408 650_2 $$2MeSH$$aHumans
000049408 650_2 $$2MeSH$$aLigands
000049408 650_2 $$2MeSH$$aLymphocyte Specific Protein Tyrosine Kinase p56(lck): chemistry
000049408 650_2 $$2MeSH$$aLymphocyte Specific Protein Tyrosine Kinase p56(lck): metabolism
000049408 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000049408 650_2 $$2MeSH$$aPeptides: metabolism
000049408 650_2 $$2MeSH$$aProtein Binding
000049408 650_2 $$2MeSH$$aProtein Structure, Tertiary
000049408 650_2 $$2MeSH$$aProto-Oncogene Proteins c-fyn: chemistry
000049408 650_2 $$2MeSH$$asrc Homology Domains
000049408 650_2 $$2MeSH$$asrc-Family Kinases: chemistry
000049408 650_7 $$00$$2NLM Chemicals$$aLigands
000049408 650_7 $$00$$2NLM Chemicals$$aPeptides
000049408 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$aFYN protein, human
000049408 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$aLymphocyte Specific Protein Tyrosine Kinase p56(lck)
000049408 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$aProto-Oncogene Proteins c-fyn
000049408 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$asrc-Family Kinases
000049408 650_7 $$2WoSType$$aJ
000049408 7001_ $$0P:(DE-HGF)0$$aSchweimer, K.$$b1
000049408 7001_ $$0P:(DE-HGF)0$$aKiessling, A.$$b2
000049408 7001_ $$0P:(DE-HGF)0$$aHofinger, E.$$b3
000049408 7001_ $$0P:(DE-HGF)0$$aBauer, F.$$b4
000049408 7001_ $$0P:(DE-Juel1)VDB630$$aHoffmann, S.$$b5$$uFZJ
000049408 7001_ $$0P:(DE-HGF)0$$aRosch, P.$$b6
000049408 7001_ $$0P:(DE-HGF)0$$aCampbell, I. D.$$b7
000049408 7001_ $$0P:(DE-HGF)0$$aWerner, J. M.$$b8
000049408 7001_ $$0P:(DE-HGF)0$$aSticht, H.$$b9
000049408 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi050814y$$gVol. 44, p. 13043 - 13050$$p13043 - 13050$$q44<13043 - 13050$$tBiochemistry$$v44$$x0006-2960$$y2005
000049408 8567_ $$uhttp://hdl.handle.net/2128/711$$uhttp://dx.doi.org/10.1021/bi050814y
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000049408 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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