Hauptseite > Publikationsdatenbank > Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity > print

001     49418
005     20200423204258.0
017 _ _ |a 0
024 7 _ |a pmid:16155203
|2 pmid
024 7 _ |a pmc:PMC2253286
|2 pmc
024 7 _ |a 10.1110/ps.051563605
|2 DOI
024 7 _ |a WOS:000232233400001
|2 WOS
024 7 _ |a 2128/2654
|2 Handle
037 _ _ |a PreJuSER-49418
041 _ _ |a eng
082 _ _ |a 610
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Bauer, F.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity
260 _ _ |a Hoboken, NJ
|b Wiley
|c 2005
300 _ _ |a 2487 -2498
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 Protein Science
|x 0961-8368
|0 10881
|y 10
|v 14
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The Src homology 3 (SH3) domain of the Src family kinase Lyn binds to the herpesviral tyrosine kinase interacting protein (Tip) more than one order of magnitude stronger than other closely related members of the Src family. In order to identify the molecular basis for high-affinity binding, the structure of free and Tip-bound Lyn-SH3 was determined by NMR spectroscopy. Tip forms additional contacts outside its classical proline-rich recognition motif and, in particular, a strictly conserved leucine (L186) of the C-terminally adjacent sequence stretch packs into a hydrophobic pocket on the Lyn surface. Although the existence of this pocket is no unique property of Lyn-SH3, Lyn is the only Src family kinase that contains an additional aromatic residue (H41) in the n-Src loop as part of this pocket. H41 covers L186 of Tip by forming tight hydrophobic contacts, and model calculations suggest that the increase in binding affinity compared with other SH3 domains can mainly be attributed to these additional interactions. These findings indicate that this pocket can mediate specificity even between otherwise closely related SH3 domains.
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 Models, Molecular
650 _ 2 |2 MeSH
|a Multiprotein Complexes: chemistry
650 _ 2 |2 MeSH
|a Multiprotein Complexes: metabolism
650 _ 2 |2 MeSH
|a Nuclear Magnetic Resonance, Biomolecular: methods
650 _ 2 |2 MeSH
|a Phosphoproteins: chemistry
650 _ 2 |2 MeSH
|a Phosphoproteins: metabolism
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Structure, Quaternary
650 _ 2 |2 MeSH
|a Viral Proteins: chemistry
650 _ 2 |2 MeSH
|a Viral Proteins: metabolism
650 _ 2 |2 MeSH
|a src Homology Domains
650 _ 2 |2 MeSH
|a src-Family Kinases: chemistry
650 _ 2 |2 MeSH
|a src-Family Kinases: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Multiprotein Complexes
650 _ 7 |0 0
|2 NLM Chemicals
|a Phosphoproteins
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 EC 2.7.10.2
|2 NLM Chemicals
|a lyn protein-tyrosine kinase
650 _ 7 |0 EC 2.7.10.2
|2 NLM Chemicals
|a src-Family Kinases
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a SH3 domain
653 2 0 |2 Author
|a Lyn
653 2 0 |2 Author
|a extended binding motif
653 2 0 |2 Author
|a ligand affinity
653 2 0 |2 Author
|a NMR
653 2 0 |2 Author
|a structure
653 2 0 |2 Author
|a complex
653 2 0 |2 Author
|a NMR spectroscopy
653 2 0 |2 Author
|a fluorescence
653 2 0 |2 Author
|a docking proteins
700 1 _ |a Schweimer, K.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Meiselbach, H.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Hoffmann, S.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB630
700 1 _ |a Rosch, P.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Sticht, H.
|b 5
|0 P:(DE-HGF)0
773 _ _ |a 10.1110/ps.051563605
|g Vol. 14, p. 2487 -2498
|p 2487 -2498
|q 14<2487 -2498
|0 PERI:(DE-600)2000025-X
|t Protein science
|v 14
|y 2005
|x 0961-8368
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2253286
856 4 _ |u https://juser.fz-juelich.de/record/49418/files/77357.pdf
|y OpenAccess
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|l Funktion und Dysfunktion des Nervensystems
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914 1 _ |y 2005
915 _ _ |0 StatID:(DE-HGF)0010
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920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
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