Related ArticlesSecondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.
Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11673-7
Authors: Overduin M, Mayer B, Rios CB, Baltimore D, Cowburn D
The Src homology 2 (SH2) domain is a recognition motif thought to mediate the association of the cytoplasmic proteins involved in signal transduction by binding to phosphotyrosyl-containing sequences in proteins. Assignments of nearly all 1H and 15N resonances of the SH2 domain from the c-Abl protein-tyrosine kinase have been obtained from homonuclear and heteronuclear NMR experiments. The secondary structure has been elucidated from the pattern of nuclear Overhauser effects, from vicinal coupling constants, and from observation of slowly exchanging amino hydrogens. The secondary structure contains two alpha-helices and eight beta-strands, six of which are arranged in two contiguous, antiparallel beta-sheets. Residues believed to be involved in phosphotyrosyl ligand binding are on a face of one beta-sheet. The alignment of homologous sequences on the basis of secondary structure suggests a conserved global fold in a family of SH2 domains.
VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy
VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy
Abstract Homology modeling is a powerful tool for predicting protein structures, whose success depends on obtaining a reasonable alignment between a given structural template and the protein sequence being analyzed. In order to leverage greater predictive power for proteins with few structural templates, we have developed a method to rank homology models based upon their compliance to secondary structure derived from experimental solid-state NMR...
[NMR paper] NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide
NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
Related Articles NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
Cell. 1998 Oct 16;95(2):269-77
Authors: Liu X, Wang H, Eberstadt M, Schnuchel A, Olejniczak ET, Meadows RP, Schkeryantz JM, Janowick DA, Harlan JE, Harris EA, Staunton DE, Fesik SW
Guanine nucleotide exchange factors for the Rho family of GTPases contain a Dbl homology (DH) domain responsible for catalysis and a...
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[NMR paper] Heteronuclear NMR assignments and secondary structure of the coiled coil trimerizatio
Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms.
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 Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced...
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[NMR paper] Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectrosco
Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectroscopy.
Biochem Biophys Res Commun. 1997 Feb 3;231(1):126-30
Authors: Miles CS, Weigelt J, Stamford NP, Dammerova N, Otting G, Dixon NE
Two separate N-terminal fragments of the 470-amino-acid Escherichia coli DnaB helicase, comprising residues 1-142 and...
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[NMR paper] Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectrosco
Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectroscopy.
Biochem Biophys Res Commun. 1997 Feb 3;231(1):126-30
Authors: Miles CS, Weigelt J, Stamford NP, Dammerova N, Otting G, Dixon NE
Two separate N-terminal fragments of the 470-amino-acid Escherichia coli DnaB helicase, comprising residues 1-142 and...
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[NMR paper] Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
Related Articles Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
Biochemistry. 1992 Aug 25;31(33):7741-4
Authors: Mott HR, Driscoll PC, Boyd J, Cooke RM, Weir MP, Campbell ID
Recombinant 15N-labeled human interleukin 2 (IL-2) has been studied by 2D and 3D NMR using uniformly 15N-labeled protein. Assignment of the backbone resonances has enabled the secondary structure of the protein to be defined. The secondary structure was...
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NMR structure of the calponin homology domain of human IQGAP1 and its implications fo
NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode
Content Type Journal Article
DOI 10.1007/s10858-010-9434-8
Authors
Ryo Umemoto, The University of Tokyo Graduate School of Pharmaceutical Sciences Hongo, Bunkyo-ku Tokyo 113-0033 Japan
Noritaka Nishida, The University of Tokyo Graduate School of Pharmaceutical Sciences Hongo, Bunkyo-ku Tokyo 113-0033 Japan
Shinji Ogino, The University of Tokyo Graduate School of Pharmaceutical Sciences Hongo, Bunkyo-ku Tokyo 113-0033 Japan
Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectrosco
Linear Mode
