Please use this identifier to cite or link to this item: https://doi.org/10.1038/emboj.2011.496
Title: Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin
Authors: Mukherjee, M.
Chow, S.Y.
Yusoff, P.
Seetharaman, J.
Ng, C.
Sinniah, S.
Koh, X.W.
Asgar, N.F.M.
Li, D.
Yim, D.
Jackson, R.A.
Yew, J.
Qian, J.
Iyu, A.
Lim, Y.P. 
Zhou, X. 
Sze, S.K.
Guy, G.R.
Sivaraman, J. 
Issue Date: 7-Mar-2012
Source: Mukherjee, M., Chow, S.Y., Yusoff, P., Seetharaman, J., Ng, C., Sinniah, S., Koh, X.W., Asgar, N.F.M., Li, D., Yim, D., Jackson, R.A., Yew, J., Qian, J., Iyu, A., Lim, Y.P., Zhou, X., Sze, S.K., Guy, G.R., Sivaraman, J. (2012-03-07). Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin. EMBO Journal 31 (5) : 1308-1319. ScholarBank@NUS Repository. https://doi.org/10.1038/emboj.2011.496
Abstract: Phosphotyrosine-binding domains, typified by the SH2 (Src homology 2) and PTB domains, are critical upstream components of signal transduction pathways. The E3 ubiquitin ligase Hakai targets tyrosine-phosphorylated E-cadherin via an uncharacterized domain. In this study, the crystal structure of Hakai (amino acids 106-206) revealed that it forms an atypical, zinc-coordinated homodimer by utilizing residues from the phosphotyrosine-binding domain of two Hakai monomers. Hakai dimerization allows the formation of a phosphotyrosine-binding pocket that recognizes specific phosphorylated tyrosines and flanking acidic amino acids of Src substrates, such as E-cadherin, cortactin and DOK1. NMR and mutational analysis identified the Hakai residues required for target binding within the binding pocket, now named the HYB domain. ZNF645 also possesses a HYB domain but demonstrates different target specificities. The HYB domain is structurally different from other phosphotyrosine-binding domains and is a potential drug target due to its novel structural features. © 2012 European Molecular Biology Organization | All Rights Reserved.
Source Title: EMBO Journal
URI: http://scholarbank.nus.edu.sg/handle/10635/77066
ISSN: 02614189
DOI: 10.1038/emboj.2011.496
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