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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A molecular ruler determines the repeat length in eukaryotic cilia and flagella.
TL;DR: Using cryo-electron tomography, it is found that FAP59 and FAP172 form a 96–nanometer (nm)–long complex in Chlamydomonas flagella and that the absence of the complex disrupted 96-nm repeats of axonemes.
Journal ArticleDOI
Sequencing and analysis of bacterial genomes
TL;DR: Sequence comparisons show that the most bacterial proteins are highly conserved in evolution, allowing predictions to be made about the functions of most products of an uncharacterized genome.
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AIRE Encodes a Nuclear Protein Co-Localizing With Cytoskeletal Filaments: Altered Sub-Cellular Distribution of Mutants Lacking the PHD Zinc Fingers
TL;DR: The sub-cellular localization of AIRE expressed transiently in COS cells and fibroblasts is investigated and it is found that AIRE has a dual nuclear and cytoplasmic localization.
Journal ArticleDOI
Molecular structure of cytoplasmic dynein 2 and its distribution in neuronal and ciliated cells.
Atsushi Mikami,Sharon H. Tynan,Taro Hama,Katherine Luby-Phelps,Tetsuichiro Saito,James E. Crandall,Joseph C. Besharse,Richard B. Vallee +7 more
TL;DR: Data support a specific role for dynein 2 in the generation and maintenance of cilia in lower eukaryotes and within primary cilia of non-neuronal cultured cells.
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Identification of Targets for Calcium Signaling through the Copine Family of Proteins: CHARACTERIZATION OF A COILED-COIL COPINE-BINDING MOTIF *
TL;DR: Evidence that copines, members of a ubiquitous family of calcium-dependent, membrane-binding proteins, may represent a universal transduction pathway for calcium signaling is provided and a consensus sequence for the coiled-coil copine-binding site was derived and found to have predictive value for identifying new copine targets.
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.