Home > Publications database > Insights into Human Lck SH3 Domain Binding Specificity: Different Binding Modes of Artificial and Native Ligands > print

001     49405
005     20200423204257.0
024 7 _ |a pmid:16274251
|2 pmid
024 7 _ |a 10.1021/bi051403k
|2 DOI
024 7 _ |a WOS:000233295900036
|2 WOS
024 7 _ |a 2128/710
|2 Handle
037 _ _ |a PreJuSER-49405
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Tran, T.
|b 0
|u FZJ
|0 P:(DE-Juel1)162212
245 _ _ |a Insights into Human Lck SH3 Domain Binding Specificity: Different Binding Modes of Artificial and Native Ligands
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2005
300 _ _ |a 15042 - 15052
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 45
|v 44
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a We analyzed the ligand binding specificity of the lymphocyte specific kinase (Lck) SH3 domain. We identified artificial Lck SH3 ligands using phage display. In addition, we analyzed Lck SH3 binding sites within known natural Lck SH3 binding proteins using an Lck specific binding assay on membrane-immobilized synthetic peptides. On one hand, from the phage-selected peptides, representing mostly special class I' ligands, a well-defined consensus sequence was obtained. Interestingly, a histidine outside the central polyproline motif contributes significantly to Lck SH3 binding affinity and specificity. On the other hand, we confirmed previously mapped Lck SH3 binding sites in ADAM15, HS1, SLP76, and NS5A, and identified putative Lck SH3 binding sites of Sam68, FasL, c-Cbl, and Cbl-b. Without exception, the comparatively diverse Lck SH3 binding sites of all analyzed natural Lck SH3 binding proteins emerged as class II proteins. Possible explanations for the observed variations between artificial and native ligands-which are not due to significant K(D) value differences as shown by calculating Lck SH3 affinities of artificial peptide PD1-Y(-3)R as well as for peptides comprising putative Lck SH3 binding sites of NS5A, Sos, and Sam68-are discussed. Our data suggest that phage display, a popular tool for determining SH3 binding specificity, must-at least in the case of Lck-not irrevocably mirror physiologically relevant protein-ligand interactions.
536 _ _ |a Neurowissenschaften
|c L01
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Consensus Sequence
650 _ 2 |2 MeSH
|a Histidine: chemistry
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 Peptide Library
650 _ 2 |2 MeSH
|a Peptides: chemistry
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Sequence Alignment
650 _ 2 |2 MeSH
|a Tyrosine: chemistry
650 _ 2 |2 MeSH
|a src Homology Domains
650 _ 7 |0 0
|2 NLM Chemicals
|a Ligands
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptide Library
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptides
650 _ 7 |0 55520-40-6
|2 NLM Chemicals
|a Tyrosine
650 _ 7 |0 71-00-1
|2 NLM Chemicals
|a Histidine
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 Hoffmann, S.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB630
700 1 _ |a Wiesehan, K.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB15437
700 1 _ |a Jonas, E.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB20019
700 1 _ |a Luge, C.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Aladag, A.
|b 5
|u FZJ
|0 P:(DE-Juel1)VDB58377
700 1 _ |a Willbold, D.
|b 6
|u FZJ
|0 P:(DE-Juel1)132029
773 _ _ |a 10.1021/bi051403k
|g Vol. 44, p. 15042 - 15052
|p 15042 - 15052
|q 44<15042 - 15052
|0 PERI:(DE-600)1472258-6
|t Biochemistry
|v 44
|y 2005
|x 0006-2960
856 7 _ |u http://dx.doi.org/10.1021/bi051403k
|u http://hdl.handle.net/2128/710
856 4 _ |u https://juser.fz-juelich.de/record/49405/files/77344.pdf
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920 1 _ |k IBI-2
|l Biologische Strukturforschung
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