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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 cellulose-deficient Arabidopsis mutant rsw3 is defective in a gene encoding a putative glucosidase II, an enzyme processing N-glycans during ER quality control.

TL;DR: Most features of the rsw3 phenotype are shared with other cellulose-deficient mutants, but some--notably, production of multiple rosettes and a lack of secreted seed mucilage--are not and may reflect glucosidase II affecting processes other than cellulose synthesis.
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Expression of nerve growth factor receptors on the ocular surface in healthy subjects and during manifestation of inflammatory diseases.

TL;DR: The authors' data support the possibility that NGF modulates ocular inflammation and corneal epithelial proliferation and differentiation through its receptors.
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Sequence and submolecular localization of the 115-kD accessory subunit of the heterotrimeric kinesin-II (KRP85/95) complex

TL;DR: The results show that kinesin and kines in-II are assembled from highly divergent accessory polypeptides together with kinesIn related motor subunits (KRPs) containing conserved motor domains linked to divergent tails and despite the lack of sequence conservation outside the motor domains, there is striking conservation of the ultrastructure of the kinesine and kinein-II holoenzymes.
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A New Syntaxin Family Member Implicated in Targeting of Intracellular Transport Vesicles

TL;DR: The cloning and initial characterization of a new member of the syntaxin family of vesicular transport receptors are reported and the sequence homology, topology, localization, and α-SNAP binding suggest that syntaxin 6 is involved in intracellular vesicle trafficking.
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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