3bd0: Difference between revisions
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'''Crystal structure of Memo, form II''' | '''Crystal structure of Memo, form II''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Qiu, C.]] | [[Category: Qiu, C.]] | ||
[[Category: | [[Category: Alpha/beta structure]] | ||
[[Category: | [[Category: Peptide binding protein]] | ||
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Revision as of 17:39, 4 May 2008
Crystal structure of Memo, form II
Overview
Memo (mediator of ErbB2-driven cell motility) is a 297-amino-acid protein recently shown to co-precipitate with the C terminus of ErbB2 and be required for ErbB2-driven cell motility. Memo is not homologous to any known signaling proteins, and how it mediates ErbB2 signals is not known. To provide a molecular basis for understanding Memo function, we have determined and report here the 2.1A crystal structure of human Memo and show it be homologous to class III nonheme iron-dependent dioxygenases, a structural class that now includes a zinc-binding protein of unknown function. No metal binding or enzymatic activity can be detected for Memo, but Memo does bind directly to a specific ErbB2-derived phosphopeptide encompassing Tyr-1227 using its vestigial enzymatic active site. Memo thus represents a new class of phosphotyrosine-binding protein.
About this Structure
3BD0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Memo Is Homologous to Nonheme Iron Dioxygenases and Binds an ErbB2-derived Phosphopeptide in Its Vestigial Active Site., Qiu C, Lienhard S, Hynes NE, Badache A, Leahy DJ, J Biol Chem. 2008 Feb 1;283(5):2734-40. Epub 2007 Nov 28. PMID:18045866 Page seeded by OCA on Sun May 4 20:39:02 2008
