Journal ArticleDOI
Predicting coiled coils from protein sequences
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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.read more
Citations
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Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division.
Quinton Tieu,Jodi Nunnari +1 more
TL;DR: The studies suggest that mitochondrial fission is a multi-step process in which Mdv2p regulates the assembly of Dnm1p into punctate structures and together with Mdv1p functions later during fission to facilitate D nm1p-dependent mitochondrial membrane constriction and/or division.
Journal ArticleDOI
tsg101: A Novel Tumor Susceptibility Gene Isolated by Controlled Homozygous Functional Knockout of Allelic Loci in Mammalian Cells
Limin Li,Stanley N. Cohen +1 more
TL;DR: Overexpression of tsg101 antisense transcripts in naive 3T3 cells resulted in cell transformation and increased stathmin-specific mRNA, a cytosolic phosphoprotein implicated previously in tumorigenesis.
Journal ArticleDOI
Structural Organization of the Synaptic Exocytosis Core Complex
TL;DR: The data indicate that syntaxin and VAMP bind primarily in a parallel arrangement and suggest a coiled-coil structure that is bent rather than fully extended, and a model in which binding of SNAP receptor (SNARE) protein co- coils domains helps drive vesicle fusion.
Journal ArticleDOI
Kinesin-related proteins required for assembly of the mitotic spindle.
TL;DR: Using a genetic screen for mutations that make KIP1 essential, another gene was identified, KSL2, which proved to be another kinesin-related gene, CIN8, which is functionally redundant: double mutants arrested in mitosis whereas the single mutants did not.
Journal ArticleDOI
Socket: a program for identifying and analysing coiled-coil motifs within protein structures
John Walshaw,Derek N. Woolfson +1 more
TL;DR: SOCKET, a computer program to identify heptad repeats of different motifs automatically in protein structures, was developed and a set of unambiguous coiled-coil structures retrieved from the RCSB Protein Data Bank was gathered.
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.
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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.
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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.
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α‐Helical coiled coils and bundles: How to design an α‐helical protein
Carolyn Cohen,David A.D. Parry +1 more
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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.