Related ArticlesSecondary structure of the homeo domain of yeast alpha 2 repressor determined by NMR spectroscopy.
Genes Dev. 1991 May;5(5):764-72
Authors: Phillips CL, Vershon AK, Johnson AD, Dahlquist FW
The yeast alpha 2 protein is a regulator of cell type in Saccharomyces cerevisiae. It represses transcription of a set of target genes by binding to an operator located upstream of each of these genes. The alpha 2 protein shares weak sequence similarity with members of the homeo domain family; the homeo domain is a 60-amino-acid segment found in many eukaryotic transcriptional regulators. In this paper we address the question of whether alpha 2 is structurally related to prototypical members of the homeo domain family. We used solution 1H and 15N nuclear magnetic resonance [NMR] spectroscopy to determine the secondary structure of an 83-amino-acid residue fragment of alpha 2 that contains the homeo domain homology. We have obtained resonance assignments for the backbone protons and nitrogens of the entire 60-residue region of the putative homeo domain and for most of the remainder of the alpha 2 fragment. The secondary structure was determined by using NOE connectivities between backbone protons, 3JHN-H alpha coupling constants, and dynamical information from the hydrogen exchange kinetics of the backbone amides. Three helical segments exist in the alpha 2 fragment consisting of residues 11-23, 32-42, and 46-60 (corresponding to residues 138-150, 159-169, and 173-187 of the intact protein). The positions of these three helices correspond extremely well to those of the Drosophila Antennapedia (Antp) and engrailed (en) homeo domains, whose three-dimensional structures have recently been determined by NMR spectroscopy and X-ray crystallography, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
[NMR paper] Pressure-dependent changes in the structure of the melittin alpha-helix determined by
Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR.
Related Articles Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR.
J Biomol NMR. 2001 Feb;19(2):115-24
Authors: Iwadate M, Asakura T, Dubovskii PV, Yamada H, Akasaka K, Williamson MP
A novel method is described, which uses changes in NMR chemical shifts to characterise the structural change in a protein with pressure. Melittin in methanol is a small alpha-helical protein, and its chemical shifts change linearly...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Three-dimensional structure of the DNA-binding domain of the fructose repressor from
Three-dimensional structure of the DNA-binding domain of the fructose repressor from Escherichia coli by 1H and 15N NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Three-dimensional structure of the DNA-binding domain of the fructose repressor from Escherichia coli by 1H and 15N NMR.
J Mol Biol. 1997 Jul 18;270(3):496-510
Authors: Penin F, Geourjon C, Montserret R, Böckmann A, Lesage A, Yang YS, Bonod-Bidaud C, Cortay JC, Nègre D, Cozzone AJ, Deléage G
FruR is...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR paper] Structure and dynamics of the lac repressor-operator complex as determined by NMR.
Structure and dynamics of the lac repressor-operator complex as determined by NMR.
Related Articles Structure and dynamics of the lac repressor-operator complex as determined by NMR.
Toxicol Lett. 1995 Dec;82-83:591-9
Authors: Kaptein R, Slijper M, Boelens R
The structures of the lac repressor headpiece and of its complex with an 11 base-pair lac half-operator have been determined by NMR spectroscopy. By 15N relaxation studies the dynamic behavior of the free protein and of the protein in the complex could be established. In the three-helical...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] Secondary structure of myristoylated recoverin determined by three-dimensional hetero
Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch.
Related Articles Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch.
Biochemistry. 1994 Sep 6;33(35):10743-53
Authors: Ames JB, Tanaka T, Stryer L, Ikura M
Recoverin, a new member of the EF-hand superfamily, serves as a Ca2+ sensor in vision. A myristoyl or related N-acyl group is covalently attached at its...
nmrlearner
Journal club
0
08-22-2010 03:29 AM
[NMR paper] Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spec
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
EMBO J. 1994 Sep 1;13(17):3936-44
Authors: Fogh RH, Ottleben G, Rüterjans H, Schnarr M, Boelens R, Kaptein R
The structure of the 84 residue DNA binding domain of the Escherichia coli LexA repressor has been determined from...
nmrlearner
Journal club
0
08-22-2010 03:29 AM
[NMR paper] 1H and 15N resonance assignment and secondary structure of capsicein, an alpha-elicit
1H and 15N resonance assignment and secondary structure of capsicein, an alpha-elicitin, determined by three-dimensional heteronuclear NMR.
Related Articles 1H and 15N resonance assignment and secondary structure of capsicein, an alpha-elicitin, determined by three-dimensional heteronuclear NMR.
Biochemistry. 1994 Jul 12;33(27):8188-97
Authors: Bouaziz S, van Heijenoort C, Huet JC, Pernollet JC, Guittet E
The backbone 1H and 15N resonance assignments and solution secondary structure determination of capsicein, a protein of 98 residues with a...
nmrlearner
Journal club
0
08-22-2010 03:29 AM
[NMR paper] Solution structure of human type-alpha transforming growth factor determined by heter
Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
Related Articles Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
Biochemistry. 1993 Jul 27;32(29):7334-53
Authors: Moy FJ, Li YC, Rauenbuehler P, Winkler ME, Scheraga HA, Montelione GT
Human type-alpha transforming growth factor (hTGF alpha) is a small mitogenic protein...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] NMR structure and functional studies of the Mu repressor DNA-binding domain.
NMR structure and functional studies of the Mu repressor DNA-binding domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure and functional studies of the Mu repressor DNA-binding domain.
Biochemistry. 1999 Jun 29;38(26):8367-76
Authors: Ilangovan U, Wojciak JM, Connolly KM, Clubb RT
The repressor protein of bacteriophage Mu establishes and maintains lysogeny by shutting down transposition functions needed for phage DNA replication. It interacts with several repeated DNA...