Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein.
Kenth Johansson,Jean-Marie Bourhis,Valérie Campanacci,Christian Cambillau,Bruno Canard,Sonia Longhi +5 more
TLDR
The crystal structure of the extreme C-terminal domain (XD) of measles virus phosphoprotein is reported, presenting the first measles virus protein structure, and light is shed on the function of the phosphop protein at the molecular level and on the process of induced folding.About:
This article is published in Journal of Biological Chemistry.The article was published on 2003-11-07 and is currently open access. It has received 156 citations till now. The article focuses on the topics: Measles Virus Nucleoprotein & Measles virus.read more
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Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling.
TL;DR: The functions of a set of well‐characterized ID regions from a diversity of proteins are presented herein to support the possibility that the relationship between amino acid sequence, disordered ensemble and function might be the dominant paradigm for the molecular recognition that serves as the basis for signaling and regulation by protein molecules.
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Natively unfolded proteins.
TL;DR: New algorithms have been developed to identify disordered regions of proteins and have demonstrated their presence in cancer-associated proteins and proteins regulated by phosphorylation.
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Assessing protein disorder and induced folding.
Véronique Receveur-Bréchot,Jean-Marie Bourhis,Vladimir N. Uversky,Vladimir N. Uversky,Bruno Canard,Sonia Longhi +5 more
TL;DR: Hints to readily recognize features typical of intrinsic disorder are provided and the principal techniques to assess structural disorder and induced folding are reviewed to point out the necessity of using different approaches and show how information can be broadened by the use of multiples techniques.
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Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins.
TL;DR: Detailed evidence is provided that ERD10 and ERD14 belong to the family of intrinsically disordered proteins, and it is shown in various assays that they act as chaperone activity of rather wide substrate specificity and that they interact with phospholipid vesicles through electrostatic forces.
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A Practical Overview of Protein Disorder Prediction Methods
TL;DR: An overview of the methods currently employed for disorder prediction highlighting their advantages and drawbacks is presented and a few practical examples of how they can be combined to avoid pitfalls and to achieve more reliable predictions are shown.
References
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Improved methods for building protein models in electron density maps and the location of errors in these models.
TL;DR: In this paper, the authors describe strategies and tools that help to alleviate this problem and simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.
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SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling.
Nicolas Guex,Manuel C. Peitsch +1 more
TL;DR: An environment for comparative protein modeling is developed that consists of SWISS‐MODEL, a server for automated comparativeprotein modeling and of the SWiss‐PdbViewer, a sequence to structure workbench that provides a large selection of structure analysis and display tools.
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Protein structure comparison by alignment of distance matrices
Liisa Holm,Chris Sander +1 more
TL;DR: A novel algorithm (DALI) for optimal pairwise alignment of protein structures that identifies structural resemblances and common structural cores accurately and sensitively, even in the presence of geometrical distortions is developed.
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The PSIPRED protein structure prediction server.
TL;DR: The PSIPRED protein structure prediction server allows users to submit a protein sequence, perform a prediction of their choice and receive the results of the prediction both textually via e-mail and graphically via the web.
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Automated MAD and MIR structure solution
TL;DR: A fully automated procedure for solving MIR and MAD structures has been developed using a scoring scheme to convert the structure-solution process into an optimization problem.