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| Home > Publications database > Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy > print |
| Home > Publications database > Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy > print |
| 001 | 49422 | ||
| 005 | 20200402210045.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:15976924 |
| 024 | 7 | _ | |2 DOI |a 10.1007/s11373-005-6797-z |
| 024 | 7 | _ | |2 WOS |a WOS:000230695300002 |
| 037 | _ | _ | |a PreJuSER-49422 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 610 |
| 084 | _ | _ | |2 WoS |a Medicine, Research & Experimental |
| 100 | 1 | _ | |a Briese, L. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy |
| 260 | _ | _ | |a London |b BioMed Central |c 2005 |
| 300 | _ | _ | |a 451 - 456 |
| 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 Journal of Biomedical Science |x 1021-7770 |0 14721 |v 12 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a The Nef protein of human immunodeficiency virus type 1 (HIV-1) is known to directly bind to the SH3 domain of human lymphocyte specific kinase (Lck) via a proline-rich region located in the amino terminal part of Nef. To address the question whether Nef binding to Lck SH3 involves residues outside the typical poly-proline peptide binding site and whether the Lck unique domain is involved in Nef-Lck interaction, we studied the direct interaction between both molecules using recombinant full-length HIV-1 Nef protein on one side and recombinantly expressed and uniformly 15N-isotope labeled Lck protein comprising unique and SH3 domains on the other side. Applying nuclear magnetic resonance spectroscopy we could show that only residues of Lck SH3, that are typically involved in binding poly-proline peptides, are affected by Nef binding. Further, for the first time we could rule out that residues of Lck unique domain are involved in binding to full length Nef protein. Thus, interactions of Lck unique domain to cellular partners e.g. CD4 or CD8, are not necessarily competitive with Lck binding to HIV-1 Nef. |
| 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 Binding Sites |
| 650 | _ | 2 | |2 MeSH |a Gene Products, nef: chemistry |
| 650 | _ | 2 | |2 MeSH |a HIV-1: chemistry |
| 650 | _ | 2 | |2 MeSH |a HIV-1: metabolism |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Lymphocyte Specific Protein Tyrosine Kinase p56(lck): chemistry |
| 650 | _ | 2 | |2 MeSH |a Magnetic Resonance Spectroscopy |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Molecular Sequence Data |
| 650 | _ | 2 | |2 MeSH |a Protein Interaction Mapping |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Receptors, Virus: metabolism |
| 650 | _ | 2 | |2 MeSH |a Recombinant Proteins |
| 650 | _ | 2 | |2 MeSH |a nef Gene Products, Human Immunodeficiency Virus |
| 650 | _ | 2 | |2 MeSH |a src Homology Domains |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Gene Products, nef |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Receptors, Virus |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Recombinant Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a nef Gene Products, Human Immunodeficiency Virus |
| 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 |
| 653 | 2 | 0 | |2 Author |a chemical shift mapping |
| 653 | 2 | 0 | |2 Author |a human immunodeficiency virus |
| 653 | 2 | 0 | |2 Author |a Lck |
| 653 | 2 | 0 | |2 Author |a ligand binding |
| 653 | 2 | 0 | |2 Author |a Nef |
| 653 | 2 | 0 | |2 Author |a nuclear magnetic resonance spectroscopy |
| 653 | 2 | 0 | |2 Author |a protein-protein interaction |
| 653 | 2 | 0 | |2 Author |a protein structure |
| 700 | 1 | _ | |a Preusser-Kunze, A. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Willbold, D. |b 2 |u FZJ |0 P:(DE-Juel1)132029 |
| 773 | _ | _ | |a 10.1007/s11373-005-6797-z |g Vol. 12, p. 451 - 456 |p 451 - 456 |q 12<451 - 456 |0 PERI:(DE-600)1482918-6 |t Journal of biomedical science |v 12 |y 2005 |x 1021-7770 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1007/s11373-005-6797-z |
| 909 | C | O | |o oai:juser.fz-juelich.de:49422 |p VDB |
| 913 | 1 | _ | |k L01 |v Neurowissenschaften |l Funktion und Dysfunktion des Nervensystems |b Leben |0 G:(DE-Juel1)FUEK255 |x 0 |
| 914 | 1 | _ | |y 2005 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k IBI-2 |l Biologische Strukturforschung |d 31.12.2006 |g IBI |0 I:(DE-Juel1)VDB58 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)77361 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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