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1sko
From Proteopedia
| 1sko, resolution 2.00Å () | |||||||||
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| Gene: | MAP2K1IP1 (Homo sapiens), MAPBPIP (Mus musculus) | ||||||||
| Domains: | MAPKK1_Int, Robl_LC7 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
MP1-p14 Complex
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1SKO is a 2 chains structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
- Lunin VV, Munger C, Wagner J, Ye Z, Cygler M, Sacher M. The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal map kinase signaling. J Biol Chem. 2004 May 28;279(22):23422-30. Epub 2004 Mar 11. PMID:15016825 doi:10.1074/jbc.M401648200
Page seeded by OCA on Wed Feb 18 04:15:42 2009
