3bd0: Difference between revisions

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caption="3bd0, resolution 3.010Å" />

'''Crystal structure of Memo, form II'''<br />

==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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BD0 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18045866 18045866]

[[Category: Homo sapiens]]

[[Category: Single protein]]

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[[Category: peptide binding protein]]

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@@ Line 2: / Line 2: @@
 caption="3bd0, resolution 3.010&Aring;" />
 '''Crystal structure of Memo, form II'''<br />
+==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==
 BD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BD0 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18045866 18045866]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
@@ Line 12: / Line 18: @@
 [[Category: peptide binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:01:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:18:55 2008''