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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Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: control of neuronal morphology.
Martijn F.B.G. Gebbink,Onno Kranenburg,Mieke Poland,Francis P.G. van Horck,Brahim Houssa,Wouter H. Moolenaar +5 more
TL;DR: A novel putative GDP/GTP exchange factor, RhoGEF (190 kD), that interacts with both wild-type and activated RhoA, but not with Rac or Cdc42, and a 116-kD protein, p116Rip, that interacting with both the GDP- and GTP-bound forms of Rho a in N1E-115 cells.
Journal ArticleDOI
LearnCoil-VMF: computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins.
TL;DR: The coiled-coil-like regions detected by LearnCoil-VMF provide further evidence that the three-stranded coiled coil is a common motif found in many diverse viral membrane-fusion proteins, suggesting that it is critical for viral-cellular membrane fusion.
Journal ArticleDOI
Identification and Characterization of a Novel Bacterial Virulence Factor That Shares Homology with Mammalian Toll/Interleukin-1 Receptor Family Proteins
TL;DR: It is demonstrated that the bacterial TIR-like protein TlpA is a novel prokaryotic modulator of NF-κB activity and IL-1β secretion that contributes to serovar Enteritidis virulence.
Journal ArticleDOI
Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically localized in the oocyte.
TL;DR: The temporal and spatial pattern of dynein accumulation in the oocytes is remarkably similar to that of several maternal effect gene products that are essential for oocyte differentiation and axis specification, lending support to recent models suggesting that microtubule motors participate in the transport of these morphogens from the nurse cell cytoplasm to the oocyte.
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Inhibition of HIV type 1 infectivity by constrained α-helical peptides: Implications for the viral fusion mechanism
J. Kevin Judice,Jeffrey Y. K. Tom,Wei Huang,Terri Wrin,Joann Vennari,Christos J. Petropoulos,Robert S. McDowell +6 more
TL;DR: The results provide a direct link between the inhibition of HIV-1 infectivity by these peptides and the x-ray structures, and suggest that the conformation of gp41 observed by crystallography represents the fusogenic state.
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.
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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.