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==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==

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[[Category: peptide binding protein]]

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@@ Line 4: / Line 4: @@
 ==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==
@@ Line 18: / Line 18: @@
 [[Category: peptide binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:18:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:04:55 2008''