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Journal ArticleDOI

Predicting coiled coils from protein sequences

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

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Citations
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The two-component hybrid kinase regulator CaNIK1 of Candida albicans.

TL;DR: Partial deletion of both CaNIK1 alleles did not inhibit either high-frequency phenotypic switching or the bud-hypha transition in high salt concentrations, but in both cases the efficiency of the developmental process was reduced.
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Structural Basis for Mitotic Centrosome Assembly in Flies.

TL;DR: These studies provide the first atomic insight into a molecular interaction required for mitotic centrosome assembly, and show that scaffold assembly requires conserved leucine zipper (LZ) and Cnn-motif 2 (CM2) domains that co-assemble into a 2:2 complex in vitro.
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Stabilizing and Destabilizing Clusters in the Hydrophobic Core of Long Two-stranded α-Helical Coiled-coils

TL;DR: The results suggested that the contribution of Leu to protein stability is context-dependent on whether the hydrophobe is in a stabilizing cluster or its proximity to neighboring destabilizing and stabilizing clusters.
Journal ArticleDOI

The small phytoplasma virulence effector SAP11 contains distinct domains required for nuclear targeting and CIN‐TCP binding and destabilization

TL;DR: The results suggest that phytoplasma effector SAP11 has a modular organization in which at least three domains are required for efficient CIN-TCP destabilization in plants.
Journal ArticleDOI

MGA2 is involved in the low-oxygen response element-dependent hypoxic induction of genes in Saccharomyces cerevisiae.

TL;DR: Analysis of results indicates that MGA2 is required for the LORE-dependent hypoxic gene induction in S. cerevisiae, and analyses using low-oxygen response element (LORE)-CYC1-lacZ fusion reporter assays and electrophoretic mobility shift assays demonstrated that Mga2 significantly affects the Lore-dependenthypoxic induction pathway of gene expression.
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.
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.
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