Journal ArticleDOI
Predicting coiled coils from protein sequences
Reads0
Chats0
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
More filters
Journal ArticleDOI
Pfam: The protein families database in 2021.
Jaina Mistry,Sara Chuguransky,Lowri Williams,Matloob Qureshi,Gustavo A. Salazar,Erik L. L. Sonnhammer,Silvio C. E. Tosatto,Lisanna Paladin,Shriya Raj,Lorna Richardson,Robert D. Finn,Alex Bateman +11 more
TL;DR: The Pfam database is a widely used resource for classifying protein sequences into families and domains and the reintroduced Pfam-B which provides an automatically generated supplement to Pfam and contains 136 730 novel clusters of sequences that are not yet matched by a Pfam family.
Journal ArticleDOI
Human non‐synonymous SNPs: server and survey
TL;DR: A World Wide Web server is presented to predict the effect of an nsSNP on protein structure and function and the dependence of selective pressure on the structural and functional properties of proteins is studied.
Journal ArticleDOI
PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization.
Kenta Nakai,Paul Horton +1 more
Journal ArticleDOI
Protein structure prediction and analysis using the Robetta server
TL;DR: The Robetta server provides automated tools for protein structure prediction and analysis and current capabilities include the prediction of the effects of mutations on protein-protein interactions using computational interface alanine scanning.
Journal ArticleDOI
ACT: the Artemis comparison tool
Tim Carver,Kim Rutherford,Matthew Berriman,Marie-Adèle Rajandream,Barclay G. Barrell,Julian Parkhill +5 more
TL;DR: The Artemis Comparison Tool (ACT) allows an interactive visualisation of comparisons between complete genome sequences and associated annotations and so inherits powerful searching and analysis tools.
References
More filters
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.
Journal ArticleDOI
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.