Related ArticlesHigh-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Science. 1994 Jul 15;265(5170):386-91
Authors: Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel beta sheet. One beta strand and one helix are contributed from each monomer. The interface between the two dimers forming the tetramer is mediated solely by helix-helix contacts. The overall result is a symmetric, four-helix bundle with adjacent helices oriented antiparallel to each other and with the two antiparallel beta sheets located on opposing faces of the molecule. The tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. The implications of the structure of the tetramer for the biological function of p53 are discussed.
[NMR paper] High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection.
High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection.
Related Articles High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection.
J Am Chem Soc. 2005 Sep 14;127(36):12528-36
Authors: Eghbalnia HR, Bahrami A, Tonelli M, Hallenga K, Markley JL
We describe a novel approach to the rapid collection and processing of multidimensional NMR data: "high-resolution iterative frequency identification for NMR" (HIFI-NMR). As with...
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[NMR paper] High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational vari
High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues.
Related Articles High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues.
J Mol Biol. 2003 Mar 21;327(2):507-20
Authors: Sprangers R, Groves MR, Sinning I, Sattler M
The SMN protein, which is linked to spinal muscular atrophy (SMA), plays an important role in the assembly of the...
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[NMR paper] High-resolution solution NMR structure of the minimal active domain of the human immu
High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Related Articles High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Biochemistry. 1998 Dec 22;37(51):17704-13
Authors: Kodera Y, Sato K, Tsukahara T, Komatsu H, Maeda T, Kohno T
The retroviral nucleocapsid (NC) protein is a multifunctional protein essential for RNA genome packaging and viral infectivity. The NC protein, NCp8, of the...
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[NMR paper] A high-resolution technique for multidimensional NMR spectroscopy.
A high-resolution technique for multidimensional NMR spectroscopy.
Related Articles A high-resolution technique for multidimensional NMR spectroscopy.
IEEE Trans Biomed Eng. 1998 Jan;45(1):78-86
Authors: Li Y, Razavilar J, Liu KJ
In this paper, a scheme for estimating frequencies and damping factors of multidimensional nuclear magnetic resonance (NMR) data is presented, multidimensional NMR data can be modeled as the sum of several multidimensional damped sinusoids. The estimated frequencies and damping factors of multidimensional NMR data...
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[NMR paper] High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
J Mol Biol. 1997 Oct 3;272(4):573-90
Authors: Tashiro M, Tejero R, Zimmerman DE, Celda B, Nilsson B, Montelione GT
Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size...
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[NMR paper] High resolution NMR solution structure of the leucine zipper domain of the c-Jun homo
High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
J Biol Chem. 1996 Jun 7;271(23):13663-7
Authors: Junius FK, O'Donoghue SI, Nilges M, Weiss AS, King GF
The solution structure of the c-Jun leucine zipper domain has been determined to high resolution using a new...
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[NMR paper] How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR s
How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X.
Related Articles How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X.
J Biol Chem. 1992 Sep 25;267(27):19642-9
Authors: Selander-Sunnerhagen M, Ullner M, Persson E, Teleman O, Stenflo J, Drakenberg T
Domains homologous to the epidermal growth factor...
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[NMR paper] High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distan
High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approach.
Related Articles High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approach.
Biochemistry. 1990 Jan 16;29(2):329-40
Authors: Summers MF, South TL, Kim B, Hare DR
A new method is described for determining molecular structures from NMR data. The approach utilizes 2D NOESY back-calculations to generate simulated spectra for structures obtained from distance geometry (DG) computations. Comparison...