4np9 | pdb_00004np9

Structure of Rabphilin C2A domain bound to IP3

spinqualitylabelsall models 4np9, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4np9 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.92Å Ligands: I3P, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RP3A_RAT Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. Publication Abstract from PubMed Proteins containing C2 domains are the sensors for Ca(2+) and PI(4,5)P2 in a myriad of secretory pathways. Here, the use of a free-mounting system has enabled us to capture an intermediate state of Ca(2+) binding to the C2A domain of rabphilin 3A that suggests a different mechanism of ion interaction. We have also determined the structure of this domain in complex with PI(4,5)P2 and IP3 at resolutions of 1.75 and 1.9 A, respectively, unveiling that the polybasic cluster formed by strands beta3-beta4 is involved in the interaction with the phosphoinositides. A comparative study demonstrates that the C2A domain is highly specific for PI(4,5)P2/PI(3,4,5)P3, whereas the C2B domain cannot discriminate among any of the diphosphorylated forms. Structural comparisons between C2A domains of rabphilin 3A and synaptotagmin 1 indicated the presence of a key glutamic residue in the polybasic cluster of synaptotagmin 1 that abolishes the interaction with PI(4,5)P2. Together, these results provide a structural explanation for the ability of different C2 domains to pull plasma and vesicle membranes close together in a Ca(2+)-dependent manner and reveal how this family of proteins can use subtle structural changes to modulate their sensitivity and specificity to various cellular signals. Structural insights into the Ca2+ and PI(4,5)P2 binding modes of the C2 domains of rabphilin 3A and synaptotagmin 1.,Guillen J, Ferrer-Orta C, Buxaderas M, Perez-Sanchez D, Guerrero-Valero M, Luengo-Gil G, Pous J, Guerra P, Gomez-Fernandez JC, Verdaguer N, Corbalan-Garcia S Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):20503-8. doi:, 10.1073/pnas.1316179110. Epub 2013 Dec 3. PMID:24302762 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exophilin Exophilin 3D structures Rabphilin

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