3bd0: Difference between revisions

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==Overview==
==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.
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==
==About this Structure==
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[[Category: peptide binding protein]]
[[Category: peptide binding protein]]


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Revision as of 17:04, 21 February 2008

File:3bd0.gif


3bd0, resolution 3.010Å

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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 with PEG as ligand. 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

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