Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.str.2010.09.014
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dc.titleStructural and functional analysis of phosphothreonine-dependent FHA domain interactions
dc.contributor.authorPennell, S.
dc.contributor.authorWestcott, S.
dc.contributor.authorOrtiz-Lombardía, M.
dc.contributor.authorPatel, D.
dc.contributor.authorLi, J.
dc.contributor.authorNott, T.J.
dc.contributor.authorMohammed, D.
dc.contributor.authorBuxton, R.S.
dc.contributor.authorYaffe, M.B.
dc.contributor.authorVerma, C.
dc.contributor.authorSmerdon, S.J.
dc.date.accessioned2014-10-27T08:40:25Z
dc.date.available2014-10-27T08:40:25Z
dc.date.issued2010-12-08
dc.identifier.citationPennell, S., Westcott, S., Ortiz-Lombardía, M., Patel, D., Li, J., Nott, T.J., Mohammed, D., Buxton, R.S., Yaffe, M.B., Verma, C., Smerdon, S.J. (2010-12-08). Structural and functional analysis of phosphothreonine-dependent FHA domain interactions. Structure 18 (12) : 1587-1595. ScholarBank@NUS Repository. https://doi.org/10.1016/j.str.2010.09.014
dc.identifier.issn09692126
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101735
dc.description.abstractFHA domains are well established as phospho-dependent binding modules mediating signal transduction in Ser/Thr kinase signaling networks in both eukaryotic and prokaryotic species. Although they are unique in binding exclusively to phosphothreonine, the basis for this discrimination over phosphoserine has remained elusive. Here, we attempt to dissect overall binding specificity at the molecular level. We first determined the optimal peptide sequence for Rv0020c FHA domain binding by oriented peptide library screening. This served as a basis for systematic mutagenic and binding analyses, allowing us to derive relative thermodynamic contributions of conserved protein and peptide residues to binding and specificity. Structures of phosphopeptide-bound and uncomplexed Rv0020c FHA domain then directed molecular dynamics simulations which show how the extraordinary discrimination in favor of phosphothreonine occurs through formation of additional hydrogen-bonding networks that are ultimately stabilized by van der Waals interactions of the phosphothreonine γ-methyl group with a conserved pocket on the FHA domain surface. © 2010 Elsevier Ltd. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.str.2010.09.014
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.str.2010.09.014
dc.description.sourcetitleStructure
dc.description.volume18
dc.description.issue12
dc.description.page1587-1595
dc.description.codenSTRUE
dc.identifier.isiut000285221100007
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