Home > Publications database > Binding, domain orientation, and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases > print

001     49408
005     20200423204257.0
024 7 _ |a pmid:16185072
|2 pmid
024 7 _ |a 10.1021/bi050814y
|2 DOI
024 7 _ |a WOS:000232253700013
|2 WOS
024 7 _ |a 2128/711
|2 Handle
037 _ _ |a PreJuSER-49408
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Hofmann, G.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Binding, domain orientation, and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2005
300 _ _ |a 13043 - 13050
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Biochemistry
|x 0006-2960
|0 798
|y 39
|v 44
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The 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.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Ligands
650 _ 2 |2 MeSH
|a Lymphocyte Specific Protein Tyrosine Kinase p56(lck): chemistry
650 _ 2 |2 MeSH
|a Lymphocyte Specific Protein Tyrosine Kinase p56(lck): metabolism
650 _ 2 |2 MeSH
|a Nuclear Magnetic Resonance, Biomolecular
650 _ 2 |2 MeSH
|a Peptides: metabolism
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Proto-Oncogene Proteins c-fyn: chemistry
650 _ 2 |2 MeSH
|a src Homology Domains
650 _ 2 |2 MeSH
|a src-Family Kinases: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Ligands
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptides
650 _ 7 |0 EC 2.7.10.2
|2 NLM Chemicals
|a FYN protein, human
650 _ 7 |0 EC 2.7.10.2
|2 NLM Chemicals
|a Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
650 _ 7 |0 EC 2.7.10.2
|2 NLM Chemicals
|a Proto-Oncogene Proteins c-fyn
650 _ 7 |0 EC 2.7.10.2
|2 NLM Chemicals
|a src-Family Kinases
650 _ 7 |a J
|2 WoSType
700 1 _ |a Schweimer, K.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Kiessling, A.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Hofinger, E.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Bauer, F.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Hoffmann, S.
|b 5
|u FZJ
|0 P:(DE-Juel1)VDB630
700 1 _ |a Rosch, P.
|b 6
|0 P:(DE-HGF)0
700 1 _ |a Campbell, I. D.
|b 7
|0 P:(DE-HGF)0
700 1 _ |a Werner, J. M.
|b 8
|0 P:(DE-HGF)0
700 1 _ |a Sticht, H.
|b 9
|0 P:(DE-HGF)0
773 _ _ |a 10.1021/bi050814y
|g Vol. 44, p. 13043 - 13050
|p 13043 - 13050
|q 44<13043 - 13050
|0 PERI:(DE-600)1472258-6
|t Biochemistry
|v 44
|y 2005
|x 0006-2960
856 7 _ |u http://dx.doi.org/10.1021/bi050814y
|u http://hdl.handle.net/2128/711
856 4 _ |u https://juser.fz-juelich.de/record/49408/files/77347.pdf
|y OpenAccess
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|l Biologische Strukturforschung
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