2CXL

RUN domain of Rap2 interacting protein x, crystallized in I422 space group

Summary for 2CXL

• Entry DOI: 10.2210/pdb2cxl/pdb
• Related: 2CXF 2DWG 2DWK
• Descriptor: rap2 interacting protein x (1 entity in total)
• Functional Keywords: run domain, helix bundle, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, protein binding
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell projection (By similarity): Q9D394
• Total number of polymer chains: 1
• Total formula weight: 21445.29

Authors

Kukimoto-Niino, M.,Umehara, T.,Murayama, K.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-06-30, release date: 2005-12-30, Last modification date: 2024-10-09)

Primary citation

Kukimoto-Niino, M.,Takagi, T.,Akasaka, R.,Murayama, K.,Uchikubo-Kamo, T.,Terada, T.,Inoue, M.,Watanabe, S.,Tanaka, A.,Hayashizaki, Y.,Kigawa, T.,Shirouzu, M.,Yokoyama, S.
Crystal Structure of the RUN Domain of the RAP2-interacting Protein x
J.Biol.Chem., 281:31843-31853, 2006

PubMed Abstract: Rap2-interacting protein x (RPIPx) is a homolog of RPIP8, a specific effector of Rap2 GTPase. The N-terminal region of RPIP8, which contains the RUN domain, interacts with Rap2. Using cell-free synthesis and NMR, we determined that the region encompassing residues 83-255 of mouse RPIPx, which is 40-residues larger than the predicted RUN domain (residues 113-245), is the minimum fragment that forms a correctly folded protein. This fragment, the RPIPx RUN domain, interacted specifically with Rap2B in vitro in a nucleotide-dependent manner. The crystal structure of the RPIPx RUN domain was determined at 2.0 A of resolution by the multiwavelength anomalous dispersion (MAD) method. The RPIPx RUN domain comprises eight anti-parallel alpha-helices, which form an extensive hydrophobic core, followed by an extended segment. The residues in the core region are highly conserved, suggesting the conservation of the RUN domain-fold among the RUN domain-containing proteins. The residues forming a positively charged surface are conserved between RPIP8 and its homologs, suggesting that this surface is important for Rap2 binding. In the crystal the putative Rap2 binding site of the RPIPx RUN domain interacts with the extended segment in a segment-swapping manner.

PubMed: 16928684
DOI: 10.1074/jbc.M604960200

Experimental method

X-RAY DIFFRACTION (3.2 Å)