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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Regulated assembly of a supramolecular centrosome scaffold in vitro
Jeffrey B. Woodruff,Oliver Wueseke,Valeria Viscardi,Julia Mahamid,Stacy D. Ochoa,Jakob Bunkenborg,Jakob Bunkenborg,Per O. Widlund,Andrei Pozniakovsky,Esther Zanin,Shirin Bahmanyar,Andrea Zinke,Sun Hae Hong,Marcus Decker,Wolfgang Baumeister,Jens S. Andersen,Karen Oegema,Anthony A. Hyman +17 more
TL;DR: The in vitro reconstitution of PCM assembly was described, found that recombinant SPD-5 could polymerize to form micrometer-sized porous networks in vitro and size and binding capacity emerge from the regulated polymerization of one coiled-coil protein to form a porous network.
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Envoplakin, a novel precursor of the cornified envelope that has homology to desmoplakin.
TL;DR: Sequence analysis showed that the 210-kD protein is homologous to the keratin- binding proteins desmoplakin, bullous pemphigoid antigen 1, and plectin, and these data suggest that the 200- kD protein may link the cornified envelope to desmosomes and keratin filaments.
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Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1
TL;DR: It is shown that human Hv1 forms a dimer in the membrane and define regions that are close to the dimer interface by using cysteine cross-linking.
Journal ArticleDOI
Chemical genetic analysis of Apg1 reveals a non-kinase role in the induction of autophagy.
TL;DR: It is found that Apg1 kinase activity is required only for Cvt trafficking of aminopeptidase I but not for import via autophagy, and the data support a novel role for ApG1 in nucleation of autophagosomes that is distinct from its catalytic kinases activity and imply a qualitative difference in the mechanism of autophile formation.
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Microtubule organization by the antagonistic mitotic motors kinesin-5 and kinesin-14
Christian Hentrich,Thomas Surrey +1 more
TL;DR: Interpolar microtubules are sorted by the directional instability resulting from antagonistic molecular motors, not a stable balance of force.
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.
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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.
Journal ArticleDOI
α‐Helical coiled coils and bundles: How to design an α‐helical protein
Carolyn Cohen,David A.D. Parry +1 more
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.