1SKO

MP1-p14 Complex

1SKO の概要

• エントリーDOI: 10.2210/pdb1sko/pdb
• 分子名称: Mitogen-activated protein kinase kinase 1 interacting protein 1, Late endosomal/lysosomal Mp1 interacting protein (3 entities in total)
• 機能のキーワード: map kinase pathway, mp1-p14 complex, scaffold proteins, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q9UHA4; Late endosome membrane; Peripheral membrane protein; Cytoplasmic side: Q9JHS3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30145.28

構造登録者

Lunin, V.V.,Munger, C.,Wagner, J.,Ye, Z.,Cygler, M.,Sacher, M. (登録日: 2004-03-05, 公開日: 2004-06-01, 最終更新日: 2024-02-14)

主引用文献

Lunin, V.V.,Munger, C.,Wagner, J.,Ye, Z.,Cygler, M.,Sacher, M.
The structure of the MAP kinase scaffold MP1 bound to its partner p14: a complex with a critical role in endosomal MAP kinase signaling
J.Biol.Chem., 279:23422-23430, 2004

PubMed Abstract: 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.

PubMed: 15016825
DOI: 10.1074/jbc.M401648200

実験手法

X-RAY DIFFRACTION (2 Å)