Related ArticlesNMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the human coactivator CBP.
Biochemistry. 2004 Feb 3;43(4):904-8
Authors: Vendel AC, Lumb KJ
Tat is required for the expression of the HIV-1 genome. HIV-1 Tat interacts with the human transcriptional coactivator and acetyltransferase CREB-binding protein (CBP) via the KIX domain of CBP. Chemical shift perturbation mapping with nuclear magnetic resonance spectroscopy was used to identify the surface of human KIX that interacts with Tat. It was found that Tat binds to the c-Jun/MLL/Tax binding surface of KIX, as opposed to the CREB binding site. The results provide new insight into the molecular basis of the assembly of protein complexes involving p300/CBP and Tat during HIV gene expression.
[NMR paper] Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscop
Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
Related Articles Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
J Biomed Sci. 2005;12(3):451-6
Authors: Briese L, Preusser A, Willbold D
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...
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[NMR paper] An NMR study of the interaction between the human copper(I) chaperone and the second
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
Related Articles An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
FEBS J. 2005 Feb;272(3):865-71
Authors: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A
The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein...
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[NMR paper] NMR assignment of human ASC2, a self contained protein interaction domain involved in
NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
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J Biomol NMR. 2002 Jun;23(2):151-2
Authors: Espejo F, Green M, Preece NE, Assa-Munt N
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[NMR paper] Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface
Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface using heteronuclear NMR methods.
Related Articles Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface using heteronuclear NMR methods.
Structure. 1999 Aug 15;7(8):919-30
Authors: Shekhtman A, McNaughton L, Cunningham RP, Baxter SM
BACKGROUND: Endonuclease III is the prototype for a family of DNA-repair enzymes that recognize and remove damaged and mismatched bases from DNA via cleavage of the N-glycosidic bond. Crystal...
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[NMR paper] NMR solution structure of a cytoplasmic surface loop of the human red cell anion tran
NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Related Articles NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Biochemistry. 1998 Aug 18;37(33):11670-8
Authors: Askin D, Bloomberg GB, Chambers EJ, Tanner MJ
The membrane domain of the human red cell anion transport protein, band 3, is too large to be studied by solution nuclear magnetic resonance spectroscopy (NMR), and its amphiphilic nature requires the use of detergents for...
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[NMR paper] NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from t
NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1.
Protein Sci. 1997 Sep;6(9):1835-48
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[NMR paper] Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution
Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods.
Related Articles Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods.
Biochemistry. 1993 Jul 6;32(26):6763-72
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational change between GDP- and GTP gamma S-bound forms of human N-ras p21. Amide...
NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the human coact
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