1sko: Difference between revisions
New page: left|200px<br /> <applet load="1sko" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sko, resolution 2.00Å" /> '''MP1-p14 Complex'''<... |
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[[Image:1sko.gif|left|200px]]<br /> | [[Image:1sko.gif|left|200px]]<br /><applet load="1sko" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1sko, resolution 2.00Å" /> | caption="1sko, resolution 2.00Å" /> | ||
'''MP1-p14 Complex'''<br /> | '''MP1-p14 Complex'''<br /> | ||
==Overview== | ==Overview== | ||
Scaffold proteins of the mitogen-activated protein kinase (MAPK) pathway | Scaffold proteins of the mitogen-activated protein kinase (MAPK) pathway have been proposed to form an active signaling module and enhance the specificity of the transduced signal. Here, we report a 2-A resolution structure of the MAPK scaffold protein MP1 in a complex with its partner protein, p14, that localizes the complex to late endosomes. The structures of these two proteins are remarkably similar, with a five-stranded beta-sheet flanked on either side by a total of three helices. The proteins form a heterodimer in solution and interact mainly through the edge beta-strand in each protein to generate a 10-stranded beta-sheet core. Both proteins also share structural similarity with the amino-terminal regulatory domains of the membrane trafficking proteins, sec22b and Ykt6p, as well as with sedlin (a component of a Golgi-associated membrane-trafficking complex) and the sigma2 and amino-terminal portion of the mu2 subunits of the clathrin adaptor complex AP2. Because neither MP1 nor p14 have been implicated in membrane traffic, we propose that the similar protein folds allow these relatively small proteins to be involved in multiple and simultaneous protein-protein interactions. Mapping of highly conserved, surface-exposed residues on MP1 and p14 provided insight into the potential sites of binding of the signaling kinases MEK1 and ERK1 to this complex, as well as the areas potentially involved in other protein-protein interactions. | ||
==About this Structure== | ==About this Structure== | ||
1SKO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | 1SKO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SKO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cygler, M.]] | [[Category: Cygler, M.]] | ||
[[Category: Lunin, V | [[Category: Lunin, V V.]] | ||
[[Category: Munger, C.]] | [[Category: Munger, C.]] | ||
[[Category: Sacher, M.]] | [[Category: Sacher, M.]] | ||
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[[Category: scaffold proteins]] | [[Category: scaffold proteins]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:32 2008'' | ||
Revision as of 16:02, 21 February 2008
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MP1-p14 Complex
OverviewOverview
Scaffold proteins of the mitogen-activated protein kinase (MAPK) pathway have been proposed to form an active signaling module and enhance the specificity of the transduced signal. Here, we report a 2-A resolution structure of the MAPK scaffold protein MP1 in a complex with its partner protein, p14, that localizes the complex to late endosomes. The structures of these two proteins are remarkably similar, with a five-stranded beta-sheet flanked on either side by a total of three helices. The proteins form a heterodimer in solution and interact mainly through the edge beta-strand in each protein to generate a 10-stranded beta-sheet core. Both proteins also share structural similarity with the amino-terminal regulatory domains of the membrane trafficking proteins, sec22b and Ykt6p, as well as with sedlin (a component of a Golgi-associated membrane-trafficking complex) and the sigma2 and amino-terminal portion of the mu2 subunits of the clathrin adaptor complex AP2. Because neither MP1 nor p14 have been implicated in membrane traffic, we propose that the similar protein folds allow these relatively small proteins to be involved in multiple and simultaneous protein-protein interactions. Mapping of highly conserved, surface-exposed residues on MP1 and p14 provided insight into the potential sites of binding of the signaling kinases MEK1 and ERK1 to this complex, as well as the areas potentially involved in other protein-protein interactions.
About this StructureAbout this Structure
1SKO is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal map kinase signaling., Lunin VV, Munger C, Wagner J, Ye Z, Cygler M, Sacher M, J Biol Chem. 2004 May 28;279(22):23422-30. Epub 2004 Mar 11. PMID:15016825
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