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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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Protease resistance of syntaxin-snap-25-vamp complexes : implications for assembly and structure

TL;DR: Results suggest that the transmembrane domains of VAMP2 and syntaxin 1A contribute to complex assembly and stability and that amino- and carboxyl-terminal regions of SNAP-25 may function as independent domains.
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The Membrane Transport Factor TAP/p115 Cycles between the Golgi and Earlier Secretory Compartments and Contains Distinct Domains Required for Its Localization and Function

TL;DR: It is shown that in interphase cells, TAP/p115 localizes predominantly to the Golgi and to peripheral structures that represent vesicular tubular clusters (VTCs) involved in ER to Golgi transport intermediates.
Journal ArticleDOI

Coiled Coils Direct Assembly of a Cold-Activated TRP Channel

TL;DR: It is shown that the TRPM8 cytoplasmic C-terminal domain contains a coiled coil that is necessary for channel assembly and sufficient for tetramer formation and a new tool that should be of general use in dissecting TRPM channel function is delineated.
Journal ArticleDOI

SPR28, a sixth member of the septin gene family in Saccharomyces cerevisiae that is expressed specifically in sporulating cells.

TL;DR: The characterization of SPR28 is reported, a sixth member of the S. cerevisiae septin gene family whose existence was revealed by the yeast genome project and exhibited specific two-hybrid interactions with itself and with three other septins that are expressed in sporulating cells.
Journal ArticleDOI

Sec35p, a Novel Peripheral Membrane Protein, Is Required for ER to Golgi Vesicle Docking

TL;DR: Using a cell-free assay that measures distinct steps in vesicle transport from the ER to the Golgi, it is found Sec35p is required for a vesicles docking stage catalyzed by Uso1p, suggesting that Sec 35p acts upstream of, or in conjunction with, Ypt1p and Sly1p as was previously found for Uso 1p.
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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