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3bcz

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[[Image:3bcz.gif|left|200px]]
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{{STRUCTURE_3bcz| PDB=3bcz | SCENE= }}
{{STRUCTURE_3bcz| PDB=3bcz | SCENE= }}
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'''Crystal structure of Memo'''
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===Crystal structure of Memo===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 18045866 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18045866}}
==About this Structure==
==About this Structure==
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[[Category: Alpha/beta structure]]
[[Category: Alpha/beta structure]]
[[Category: Peptide binding protein]]
[[Category: Peptide binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:38:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:59:41 2008''

Revision as of 22:59, 27 July 2008

Template:STRUCTURE 3bcz

Crystal structure of Memo

Template:ABSTRACT PUBMED 18045866

About this Structure

3BCZ 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

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