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Data on Proteomics Described by Researchers at University of California (Achieving peptide binding specificity and promiscuity by loops: case of the...

August 12, 2014



Data on Proteomics Described by Researchers at University of California (Achieving peptide binding specificity and promiscuity by loops: case of the forkhead-associated domain)

By a News Reporter-Staff News Editor at Life Science Weekly -- New research on Proteomics is the subject of a report. According to news reporting out of Riverside, California, by NewsRx editors, research stated, "The regulation of a series of cellular events requires specific protein-protein interactions, which are usually mediated by modular domains to precisely select a particular sequence from diverse partners. However, most signaling domains can bind to more than one peptide sequence."

Our news journalists obtained a quote from the research from the University of California, "How do proteins create promiscuity from precision? Moreover, these complex interactions typically occur at the interface of a well-defined secondary structure, ? helix and ? sheet. However, the molecular recognition primarily controlled by loop architecture is not fully understood. To gain a deep understanding of binding selectivity and promiscuity by the conformation of loops, we chose the forkhead-associated (FHA) domain as our model system. The domain can bind to diverse peptides via various loops but only interact with sequences containing phosphothreonine (pThr). We applied molecular dynamics (MD) simulations for multiple free and bound FHA domains to study the changes in conformations and dynamics. Generally, FHA domains share a similar folding structure whereby the backbone holds the overall geometry and the variety of sidechain atoms of multiple loops creates a binding surface to target a specific partner. FHA domains determine the specificity of pThr by well-organized binding loops, which are rigid to define a phospho recognition site. The broad range of peptide recognition can be attributed to different arrangements of the loop interaction network. The moderate flexibility of the loop conformation can help access or exclude binding partners."

According to the news editors, the research concluded: "Our work provides insights into molecular recognition in terms of binding specificity and promiscuity and helpful clues for further peptide design."

For more information on this research see: Achieving peptide binding specificity and promiscuity by loops: case of the forkhead-associated domain. Plos One, 2014;9(5):e98291. (Public Library of Science - www.plos.org; Plos One - www.plosone.org)

Our news journalists report that additional information may be obtained by contacting Y.M. Huang, Dept. of Chemistry, University of California Riverside, Riverside, California, United States (see also Proteomics).

Keywords for this news article include: Peptides, Proteins, Riverside, California, Proteomics, United States, Nanotechnology, Emerging Technologies, Molecular Recognition, North and Central America.

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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