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
Journal ArticleDOI

Modulation of Receptor Recycling and Degradation by the Endosomal Kinesin KIF16B

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.

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.
Journal ArticleDOI

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
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)