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Protein Homology/analogY Recognition Engine V 2.2 |
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Welcome to the Phyre2.2 Help page. Phyre2.2 is an update to Phyre2. It should run faster, and uses a new fold library based on UniProt entries rather than on SCOP domains. The original Phyre2 algorithm and fold library will still be available via an option on the home page. As with Phyre2, the new system is designed around the idea that you have a protein sequence/gene and want to predict its three-dimensional (3D) structure. Whereas Phyre2 produced the alignment of hidden Markov models via HHsearch1, Phyre2.2 uses the faster program HHBlits2, which comes from the same laboratory; in spite of running up to ~100 times faster, it gives comparable results. Phyre2.2 presents the results in a slightly different way than Phyre2; rather than being strictly in order of increasing E-values as reported by HHBlits (or HHSearch), the results are analysed to distinguish different domains, and these are grouped together at the top of the list. The new fold library contains templates for both apo- and holo- proteins with the same sequence. This results in models for both, which can be useful when studying the binding modes of proteins to ligans, for example. Because the AlphaFold DB with over 220,000,000 models is now available, we have implemented a function to allow one-to-one threading using this database. One-to-one threading allows the user to build a model for their sequence based on a single template; previously the user had to supply a PDB file (derived from the PDB itself or perhaps from an unpublished in-house structure), but now the sequence can be aligned against all entries in the Alphafold DB and the best fit used as a template. If you are completely new to the ideas of protein structure prediction the video below will give you a very brief overview of the general technique. More videos will be available soon from the "Video Tutorials" link above. |
Full Lecture |
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A full 1hr45m lecture by Lawrence Kelley on protein structure prediction and how
Phyre works in more detail is
available: EBI Lecture 2018 |
References | |
1. Söding J. (2005) Protein homology detection by HMM-HMM comparison. Bioinformatics 21, 951-960. doi:10.1093/bioinformatics/bti125. | |
2. Remmert M, Biegert A, Hauser A, & Söding J. (2012) HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment. Nature Methods 9, 173–175. doi:10.1038/nmeth.1818 |
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Missense3D Portal: | a suite of resources for the analysis of amino acid substitutions in proteins |
GWYRE: | contains modeled and experimentally determined structures of human proteins and protein complexes, annotated by phenotypic effects of genetic mutations. |
Phyre is now FREE for commercial users!
All images and data generated by Phyre2 are free to use in any publication with acknowledgement
Accessibility StatementPlease cite: The Phyre2 web portal for protein modeling, prediction and analysis | ||
Kelley LA et al. Nature Protocols 10, 845-858 (2015) [paper] [Citation link] | ||
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