5KHO

Rasip1 RA domain in complex with Rap1B

Summary for 5KHO

• Entry DOI: 10.2210/pdb5kho/pdb
• Related: 5KHQ
• Descriptor: Ras-interacting protein 1, Ras-related protein Rap-1b, GLYCEROL, ... (6 entities in total)
• Functional Keywords: rasip1, ras-association domain, rap1b, complex, signaling protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, perinuclear region : Q5U651; Cell membrane: P61224
• Total number of polymer chains: 4
• Total formula weight: 71916.73

Authors

Gingras, A.R. (deposition date: 2016-06-15, release date: 2016-10-19, Last modification date: 2023-09-27)

Primary citation

Gingras, A.R.,Puzon-McLaughlin, W.,Bobkov, A.A.,Ginsberg, M.H.
Structural Basis of Dimeric Rasip1 RA Domain Recognition of the Ras Subfamily of GTP-Binding Proteins.
Structure, 24:2152-2162, 2016

PubMed Abstract: Ras-interacting protein 1 (Rasip1) is an endothelial-specific Rap1 and Ras effector, important for vascular development and angiogenesis. Here, we report the crystal structure of the Rasip1 RA domain (RRA) alone, revealing the basis of dimerization, and in complex with Rap1 at 2.8 Å resolution. In contrast to most RA domains, RRA formed a dimer that can bind two Rap1 (K = 0.9 μM) or Ras (K = 2.2 μM) molecules. We solved the Rap1-RRA complex and found that Rasip1 binds Rap1 in the Switch I region, and Rap1 binding induces few conformation changes to Rasip1 stabilizing a β strand and an unstructured loop. Our data explain how Rasip1 can act as a Rap1 and Ras effector and show that Rasip1 defines a subgroup of dimeric RA domains that could mediate cooperative binding to membrane-associated Ras superfamily members.

PubMed: 27839947
DOI: 10.1016/j.str.2016.10.001

Experimental method

X-RAY DIFFRACTION (2.78 Å)