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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Non-globular domains in protein sequences: automated segmentation using complexity measures.
TL;DR: The SEG algorithm provides an effective general method for partitioning the globular and non-globular regions of these sequences fully automatically, facilitating the discovery of new classes of long, non-Globular sequence segments, as illustrated by the example of the human CAN gene product involved in tumor induction.
Journal ArticleDOI
NUDEL is a novel Cdk5 substrate that associates with LIS1 and cytoplasmic dynein.
Martin Niethammer,Deanna S. Smith,Ramses Ayala,Junmin Peng,Jane Ko,Ming-Sum Lee,Maria A. Morabito,Li-Huei Tsai,Li-Huei Tsai +8 more
TL;DR: NUDEL is a novel LIS1-interacting protein with sequence homology to gene products also implicated in nuclear distribution in fungi and is a substrate of Cdk5, a kinase known to be critical during neuronal migration.
Journal ArticleDOI
Identification and mutation analysis of the complete gene for Chediak-Higashi syndrome.
Deborah L. Nagle,Mohammad A. Karim,Elizabeth A. Woolf,Lisa Holmgren,Peer Bork,Donald J. Misumi,Sonja H. McGrail,Barry J. Dussault,Charles M. Perou,Raymond E. Boissy,Geoffrey M. Duyk,Richard A. Spritz,Karen J. Moore +12 more
TL;DR: Analysis of the CHS polypeptide demonstrates that its modular architecture is similar to the yeast vacuolar sorting protein, VPS15, and this work describes the sequence of a human cDNA homologous to mouse beige, identify pathologic mutations and clarify the discrepancies of the previous reports.
Journal ArticleDOI
The septins: Roles in cytokinesis and other processes
Mark S. Longtine,Douglas J. Demarini,Maria L. Valencik,Omayma S Al-Awar,Hanna Fares,Claudio De Virgilio,John R. Pringle +6 more
TL;DR: The septins are a novel family of proteins that were first recognized in yeast as proteins associated with the neck filaments and appear to be essential for this process in both fungal and animal cells.
Journal ArticleDOI
Performance of mutation pathogenicity prediction methods on missense variants.
TL;DR: The overall best performing methods in this study were SNPs&GO and MutPred, with accuracies reaching 0.82 and 0.81, respectively.
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
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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.