ArticleJournal of molecular modeling2006
Determining functionally important amino acid residues of the E1 protein of Venezuelan equine encephalitis virus.
Article in Journal of molecular modeling, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
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- NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.Journal of structural and functional genomics · 2010Article
- Structural analysis of linear and conformational epitopes of allergens.Regulatory toxicology and pharmacology : RTP · 2009Review
- Automated detection of conformational epitopes using phage display Peptide sequences.Bioinformatics and biology insights · 2009Article
- Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains.Proteins · 2009Article
- Identification and analysis of conserved sequence motifs in cytochrome P450 family 2. Functional and structural role of a motif 187RFDYKD192 in CYP2B enzymes.The Journal of biological chemistry · 2008Article
- Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150).The Journal of biological chemistry · 2008Article
- Co-localization of glyceraldehyde-3-phosphate dehydrogenase with ferredoxin-NADP reductase in pea leaf chloroplasts.Journal of structural biology · 2008Article
- InterProSurf: a web server for predicting interacting sites on protein surfaces.Bioinformatics (Oxford, England) · 2007Article
- Statistical analysis of physical-chemical properties and prediction of protein-protein interfaces.Journal of molecular modeling · 2007Article
- Flavitrack: an annotated database of flavivirus sequences.Bioinformatics (Oxford, England) · 2007Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A new method for predicting interacting residues in protein complexes, InterProSurf, was applied to the E1 envelope protein of Venezuelan equine encephalitis (VEEV). Monomeric and trimeric models of VEEV-E1 were constructed with our MPACK program, using the crystal structure of the E1 protein of Semliki forest virus as a template. An alignment of the E1 sequences from representative alphavirus sequences was used to determine physical chemical property motifs (likely functional areas) with our PCPMer program. Information on residue variability, propensity to be in protein interfaces, and surface exposure on the model was combined to predict surface clusters likely to interact with other viral or cellular proteins. Mutagenesis of these clusters indicated that the predictions accurately detected areas crucial for virus infection. In addition to the fusion peptide area in domain 2, at least two other surface areas play an important role in virus infection. We propose that these may be sites of interaction between the E1-E1 and E1-E2 subdomains of the envelope proteins that are required to assemble the functional unit. The InterProSurf method is, thus, an important new tool for predicting viral protein interactions. These results can aid in the design of new vaccines against alphaviruses and other viruses.
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