4QAM

Crystal Structure of the RPGR RCC1-like domain in complex with the RPGR-interacting domain of RPGRIP1

Summary for 4QAM

• Entry DOI: 10.2210/pdb4qam/pdb
• Descriptor: X-linked retinitis pigmentosa GTPase regulator, X-linked retinitis pigmentosa GTPase regulator-interacting protein 1, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: type ii c2 domain, beta propeller, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytoskeleton, flagellum axoneme . Isoform 6: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome: Q92834; Cell projection, cilium : Q96KN7
• Total number of polymer chains: 2
• Total formula weight: 67431.34

Authors

Remans, K.,Buerger, M.,Vetter, I.R.,Wittinghofer, A. (deposition date: 2014-05-05, release date: 2014-07-30, Last modification date: 2024-11-27)

Primary citation

Remans, K.,Burger, M.,Vetter, I.R.,Wittinghofer, A.
C2 domains as protein-protein interaction modules in the ciliary transition zone.
Cell Rep, 8:1-9, 2014

PubMed Abstract: RPGR-interacting protein 1 (RPGRIP1) is mutated in the eye disease Leber congenital amaurosis (LCA) and its structural homolog, RPGRIP1-like (RPGRIP1L), is mutated in many different ciliopathies. Both are multidomain proteins that are predicted to interact with retinitis pigmentosa G-protein regulator (RPGR). RPGR is mutated in X-linked retinitis pigmentosa and is located in photoreceptors and primary cilia. We solved the crystal structure of the complex between the RPGR-interacting domain (RID) of RPGRIP1 and RPGR and demonstrate that RPGRIP1L binds to RPGR similarly. RPGRIP1 binding to RPGR affects the interaction with PDEδ, the cargo shuttling factor for prenylated ciliary proteins. RPGRIP1-RID is a C2 domain with a canonical β sandwich structure that does not bind Ca(2+) and/or phospholipids and thus constitutes a unique type of protein-protein interaction module. Judging from the large number of C2 domains in most of the ciliary transition zone proteins identified thus far, the structure presented here seems to constitute a cilia-specific module that is present in multiprotein transition zone complexes.

PubMed: 24981858
DOI: 10.1016/j.celrep.2014.05.049

Experimental method

X-RAY DIFFRACTION (1.83 Å)