Related ArticlesDetermination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element.
J Biomol NMR. 1998 Jan;11(1):59-84
Authors: Howe PW, Allain FH, Varani G, Neuhaus D
RNA-protein recognition is critical to post-transcriptional regulation of gene expression, yet poorly understood at the molecular level. The relatively slow progress in understanding this important area of molecular biology is due to difficulties in obtaining good-quality crystals and derivatives, and in preparing samples suitable for NMR investigation. The determination of the structure of the complex between the human U1A protein and its polyadenylation inhibition element is described here. In this paper, we describe the sample preparation, spectral assignments, construction of the NOE-based distance constraints and methodology for calculating the structure of the complex. The structure was determined to an overall precision of 2.03 A (for all ordered regions), and 1.08 A for the protein-RNA interface. The patterns of hydrogen bonding and hydrophobic interactions at the interface were analysed statistically using the final ensemble of 31 structures.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
Top Curr Chem. 2011 Aug 2;
Authors: Vinogradova O, Qin J
Protein-protein interactions are crucial for a wide variety of biological processes. These interactions range from high affinity (K (d) < nM) to very low affinity (K (d) > mM). While much is known about the nature of high affinity protein complexes, our knowledge about structural characteristics...
nmrlearner
Journal club
0
08-03-2011 12:00 PM
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Related Articles Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Structure. 2010 Dec 8;18(12):1678-1687
Authors: Masica DL, Ash JT, Ndao M, Drobny GP, Gray JJ
Protein-biomineral interactions are paramount to materials production in biology, including the mineral phase of hard tissue. Unfortunately, the...
nmrlearner
Journal club
0
12-08-2010 06:21 PM
[NMR paper] The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of co
The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Related Articles The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Nat Struct Biol. 2000 Apr;7(4):329-35
Authors: Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G
The status of the poly(A) tail at the 3'-end of mRNAs controls the expression of numerous genes in response to...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and ind
The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition.
Related Articles The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition.
EMBO J. 1999 Nov 15;18(22):6508-21
Authors: Stoldt M, Wöhnert J, Ohlenschläger O, Görlach M, Brown LR
The structure of the complex between ribosomal protein L25 and a 37 nucleotide RNA molecule, which contains the E-loop and helix IV regions of the E-domain of Escherichia coli 5S rRNA, has been determined to an overall...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine
NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes.
Related Articles NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes.
Biochemistry. 1999 Oct 5;38(40):12984-94
Authors: Schüler W, Dong C, Wecker K, Roques BP
The structure of the 56 amino acid nucleocapsid protein NCp10 of...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-
Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-binding domain.
Related Articles Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-binding domain.
J Biomol NMR. 1995 Nov;6(3):294-305
Authors: Morikawa S, Ogata K, Sekikawa A, Sarai A, Ishii S, Nishimura Y, Nakamura H
The solution structure of a specific DNA complex of the minimum DNA-binding domain of the mouse c-Myb protein was determined by distance geometry calculations using a set of 1732 nuclear Overhauser enhancement...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] Determination of the backbone mobility of ribonuclease T1 and its 2'GMP complex using
Determination of the backbone mobility of ribonuclease T1 and its 2'GMP complex using molecular dynamics simulations and NMR relaxation data.
Related Articles Determination of the backbone mobility of ribonuclease T1 and its 2'GMP complex using molecular dynamics simulations and NMR relaxation data.
J Biomol Struct Dyn. 1994 Jun;11(6):1377-402
Authors: Fushman D, Ohlenschläger O, Rüterjans H
The results of 1-nanosecond molecular dynamics simulations of the enzyme ribonuclease T1 and its 2'GMP complex in water are presented. A classification...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Determination of the backbone mobility of ribonuclease T1 and its 2'GMP complex using
Determination of the backbone mobility of ribonuclease T1 and its 2'GMP complex using molecular dynamics simulations and NMR relaxation data.
Related Articles Determination of the backbone mobility of ribonuclease T1 and its 2'GMP complex using molecular dynamics simulations and NMR relaxation data.
J Biomol Struct Dyn. 1994 Jun;11(6):1377-402
Authors: Fushman D, Ohlenschläger O, Rüterjans H
The results of 1-nanosecond molecular dynamics simulations of the enzyme ribonuclease T1 and its 2'GMP complex in water are presented. A classification...
Determination of the NMR structure of the complex between U1A protein and its RNA pol
Linear Mode
