1sko
MP1-p14 Complex
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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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