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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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New Knowledge from Old: In silico discovery of novel protein domains in Streptomyces coelicolor

TL;DR: Delineation of protein domain families enables detailed analysis of protein function, as well as identification of likely regions or residues of particular interest, and is demonstrated to fairly rapidly generate new biological information from previously uncorrelated data.
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cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane.

TL;DR: Immunoblot analysis of mouse P19 teratocarcinoma cells and the P19MES-differentiated derivative of the latter suggest that LAP1 isotypes are differentially expressed during development, similar to members of the nuclear lamin family.
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Multi-genome identification and characterization of chlamydiae-specific type III secretion substrates: the Inc proteins.

TL;DR: The abundance of segments with a high probability for coiled coil conformation in Inc proteins support the hypothesis that they interact with host proteins, and suggest the novel finding that translocation of Inc proteins may be regulated by as-yet undetermined mechanisms.
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Natural competence for DNA transformation in Helicobacter pylori : identification and genetic characterization of the comB locus

TL;DR: The comB gene locus of H. pylori is described, which consists of a cluster of four tandemly arranged genes with partially overlapping open reading frames constituting a single transcriptional unit involved in DNA transformation competence.
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Yeast Num1p associates with the mother cell cortex during S/G2 phase and affects microtubular functions.

TL;DR: The data suggest that the periodically expressed NUM1 gene product controls nuclear migration by affecting astral microtubule functions.
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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