Journal ArticleDOI
Predicting coiled coils from protein sequences
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TLDR
This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled -coil structures,such as the hinge region in myosin.Abstract:
The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.read more
Citations
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Modulation of Receptor Recycling and Degradation by the Endosomal Kinesin KIF16B
Sebastian Hoepfner,Fedor F. Severin,Alicia Cabezas,Bianca Habermann,Anja Runge,David J. Gillooly,Harald Stenmark,Marino Zerial +7 more
TL;DR: KIF16B, by regulating the plus end motility of early endosomes, modulates the intracellular localization of earlyendosomes and the balance between receptor recycling and degradation and it is proposed that this mechanism could have important implications for signaling.
Journal ArticleDOI
Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer.
TL;DR: Comparisons of the domain distributions in eukaryotes and prokaryotes enabled distinctions to be made between the domains originating prior to the last common ancestor of all known life forms and those apparently originating as consequences of horizontal gene transfer events.
Journal ArticleDOI
slow border cells, a locus required for a developmentally regulated cell migration during oogenesis, encodes Drosophila C/EBP.
TL;DR: The slbo locus was found to encode a product homologous to the CCAAT/enhancer-binding protein (C/EBP), a basic region-leucine zipper transcription factor, which may be required for the expression of gene products mediating border cell migration in Drosophila.
Journal ArticleDOI
Identification and characterization of the STIM (stromal interaction molecule) gene family: coding for a novel class of transmembrane proteins.
Richard T. Williams,Shehnaaz S.M. Manji,Nigel J. Parker,Manuela S. Hancock,Leonie van Stekelenburg,Jean-Pierre Eid,Paul V. Senior,Janette S. Kazenwadel,Tetyana Shandala,Robert Saint,Peter J. Smith,Marie Dziadek +11 more
TL;DR: It is demonstrated by mutation analysis and protein sequencing that human STIM2 initiates translation exclusively from a non-AUG start site in vivo, indicating a possible functional interaction between STIM1 and STIM 2.
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Isolation and analysis of xlnR, encoding a transcriptional activator co‐ordinating xylanolytic expression in Aspergillus niger
TL;DR: The results indicate that XlnR is a transcriptional activator of the xylanolytic system in A. niger and may be an important and conserved cis‐acting element in induction of x Dylanolytic genes in filamentous fungi
References
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Journal ArticleDOI
The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
TL;DR: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
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Evidence that the leucine zipper is a coiled coil
TL;DR: A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and characterized and associates in the micromolar concentration range to form a very stable dimer of alpha helices with a parallel orientation.
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Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA.
TL;DR: The putative DNA-binding domain of CREB is structurally similar to the corresponding domains in the phorbol ester-responsive c-jun protein and the yeast transcription factor GCN4.
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α‐Helical coiled coils and bundles: How to design an α‐helical protein
Carolyn Cohen,David A.D. Parry +1 more
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A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
TL;DR: The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 Å resolution, is described, and is the first representative of a second class of aminoacyl-tRNA synthet enzyme structures.