Hauptseite > Publikationsdatenbank > Characterization of Lck-binding elements in the herpesviral regulatory Tip protein > print

001     46280
005     20200423204152.0
024 7 _ |a pmid:15554700
|2 pmid
024 7 _ |a 10.1021/bi0485068
|2 DOI
024 7 _ |a WOS:000225353300007
|2 WOS
024 7 _ |a 2128/707
|2 Handle
037 _ _ |a PreJuSER-46280
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Bauer, F.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Characterization of Lck-binding elements in the herpesviral regulatory Tip protein
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2004
300 _ _ |a 14932-9
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 47
|v 43
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Herpesvirus saimiri encodes a tyrosine kinase interacting protein (Tip) that binds to T-cell-specific tyrosine kinase Lck via multiple sequence motifs and controls its activity. The regulation of Lck by Tip represents a key mechanism in the transformation of human T-lymphocytes during herpesviral infection. In this study, the interaction of Tip with the regulatory SH3 and SH2 domains of Lck was investigated by biophysical and computational techniques. NMR spectroscopy of isotopically labeled Tip(140-191) revealed that the interaction with the LckSH3 domain is not restricted to the classical proline-rich motif, but also involves the C-terminally adjacent residues which pack into a hydrophobic pocket on the surface of the SH3 domain, thus playing a likely role in mediating binding specificity. Fluorescence binding studies of Tip further demonstrate that Tyr127 in its phosphorylated form represents a strong ligand of the LckSH2 domain, indicating the presence of an additional Lck interaction motif. In contrast, Tyr114, known to be essential for STAT-3 binding, does not interact with the LckSH2 domain, showing that the tyrosines in Tip exhibit distinct binding specificity. The existence of numerous interaction sites between Tip and the regulatory domains of Lck implies a complex regulatory mechanism and may have evolved to allow a gradual regulation of Lck activity in different pathogenic states.
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 Amino Acid Sequence
650 _ 2 |2 MeSH
|a Circular Dichroism
650 _ 2 |2 MeSH
|a Cloning, Molecular
650 _ 2 |2 MeSH
|a Conserved Sequence
650 _ 2 |2 MeSH
|a Herpesvirus 2, Saimiriine: chemistry
650 _ 2 |2 MeSH
|a Herpesvirus 2, Saimiriine: enzymology
650 _ 2 |2 MeSH
|a Herpesvirus 2, Saimiriine: metabolism
650 _ 2 |2 MeSH
|a Hydrophobic and Hydrophilic Interactions
650 _ 2 |2 MeSH
|a Kinetics
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 Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Nuclear Magnetic Resonance, Biomolecular
650 _ 2 |2 MeSH
|a Phosphoproteins: chemistry
650 _ 2 |2 MeSH
|a Phosphoproteins: genetics
650 _ 2 |2 MeSH
|a Phosphoproteins: isolation & purification
650 _ 2 |2 MeSH
|a Phosphoproteins: metabolism
650 _ 2 |2 MeSH
|a Phosphotyrosine: chemistry
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Protons
650 _ 2 |2 MeSH
|a Sequence Homology, Amino Acid
650 _ 2 |2 MeSH
|a Spectrometry, Fluorescence
650 _ 2 |2 MeSH
|a Viral Proteins: chemistry
650 _ 2 |2 MeSH
|a Viral Proteins: genetics
650 _ 2 |2 MeSH
|a Viral Proteins: isolation & purification
650 _ 2 |2 MeSH
|a Viral Proteins: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Ligands
650 _ 7 |0 0
|2 NLM Chemicals
|a Phosphoproteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Protons
650 _ 7 |0 0
|2 NLM Chemicals
|a Viral Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a tyrosine kinase interacting protein, Saimiriine herpesvirus 2
650 _ 7 |0 21820-51-9
|2 NLM Chemicals
|a Phosphotyrosine
650 _ 7 |0 EC 2.7.10.2
|2 NLM Chemicals
|a Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
650 _ 7 |a J
|2 WoSType
700 1 _ |a Hofinger, E.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Hoffmann, S.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB630
700 1 _ |a Rösch, P.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Schweimer, K.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Sticht, H.
|b 5
|0 P:(DE-HGF)0
773 _ _ |a 10.1021/bi0485068
|g Vol. 43, p. 14932-9
|p 14932-9
|q 43<14932-9
|0 PERI:(DE-600)1472258-6
|t Biochemistry
|v 43
|y 2004
|x 0006-2960
856 7 _ |u http://dx.doi.org/10.1021/bi0485068
|u http://hdl.handle.net/2128/707
856 4 _ |u https://juser.fz-juelich.de/record/46280/files/72895.pdf
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909 C O |o oai:juser.fz-juelich.de:46280
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913 1 _ |k L01
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920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
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