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
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Comprehensive sequence analysis of the 182 predicted open reading frames of yeast chromosome III
Peer Bork,Christos A. Ouzounis,Chris Sander,Michael Scharf,Reinhard Schneider,Erik L. L. Sonnhammer +5 more
TL;DR: It is suggested that the development of an automated computer workbench for protein sequence analysis must be an important item in genome projects because the information gap between known protein sequences and unknown function is expected to widen and become a major bottleneck of genome projects in the near future.
Journal ArticleDOI
Domain-specific Interaction with the IκB Kinase (IKK) Regulatory Subunit IKKγ Is an Essential Step in Tax-mediated Activation of IKK
TL;DR: It is shown that the Tax-IKKγ interaction requires two homologous leucine zipper domains located within IKKγ, which are unique for the presence of a conserved upstream region that is essential for Tax binding.
Journal ArticleDOI
Activity of the Human Centrosomal Kinase, Nek2, Depends on an Unusual Leucine Zipper Dimerization Motif
TL;DR: This study reveals not only an important mechanism for the regulation of the Nek2 kinase but, furthermore, highlights an unusual organization of a leucine zipper dimerization motif.
Journal ArticleDOI
Identification of a novel gene, FGFR1OP2, fused to FGFR1 in 8p11 myeloproliferative syndrome.
Effie K. Grand,Effie K. Grand,Francis H. Grand,Francis H. Grand,Andrew Chase,Andrew Chase,Fiona M. Ross,Fiona M. Ross,Martin Corcoran,David Oscier,Nicholas C.P. Cross,Nicholas C.P. Cross +11 more
TL;DR: The identification of a new FGFR1 fusion gene in a patient who presented with T‐cell lymphoblastic lymphoma in conjunction with an acquired ins(12;8)(p11;p11p22) and the presence of the chimeric gene was confirmed by RT‐PCR, genomic DNA PCR, and FISH, which further support the central role of deregulatedFGFR1 in the pathogenesis of EMS.
Journal ArticleDOI
Flagellar radial spokes contain a Ca2+-stimulated nucleoside diphosphate kinase.
TL;DR: It is concluded that p61 is an integral component of the radial spoke stalk that binds calmodulin and exhibits Ca(2+)-controlled NDKase activity, suggesting that nucleotides other than ATP may play an important role in the signal transduction pathway that underlies the regulatory mechanism defined by the radial spokes.
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.