scispace - formally typeset
Journal ArticleDOI

Predicting coiled coils from protein sequences

Andrei N. Lupas, +2 more
- 24 May 1991 - 
- Vol. 252, Iss: 5009, pp 1162-1164
Reads0
Chats0
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
More filters

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.
Journal ArticleDOI

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.

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.
Journal ArticleDOI

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
More filters
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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Related Papers (5)