Rabphilin: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky

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-<StructureSection load='3d2d' size='340' side='right' caption='Structure of glycosylated California poppy reticuline oxidase complex with reticuline and FAD (PDB code [[3d2d]])' scene='87/873793/Cv/1'>
+<StructureSection load='5lob' size='340' side='right' caption='Structure of rabphilin-3A C2B domain  (green, grey, pink) complex with SNAP-25 N-terminal helix (yellow, magenta), glycerol, sulfate and Ca+2 ions (PDB code [[5lob]])' scene='87/873795/Cv/1'>
 == Function ==
-'''Rabphilin''' or '''berberine bridge-forming enzyme''' (RO) is part of the alkaloids biosynthesis pathway catalyzing the conversion of (S)-reticuline to (S)-scoulerine<ref>PMID:1946465</ref>.  RO catalyzes the cyclization of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon, C-8 of (S)- <ref>PMID:7592663</ref>.
+'''Rabphilin''' (Rab) is known as a synaptic vesicle-associated protein involved in the regulation of exo- and endocytosis processes at presynaptic sites<ref>PMID:26679993</ref>.
 == Relevance ==
-Reticuline is a precursor of morphine and has potent central nervous system depressing effects<ref>PMID:9720612</ref>.
+Rab is a major auto antigen in lymphocytic infundibulo-neurohypophysitis (LINH). Antibodies to Rab may serve as a biomarker for the diagnosis of LINH<ref>PMID:25919460</ref>.
 == Structural highlights ==
-The 3D structure of the complex between RO and its substrate reticuline show the cofactor FAD having bicovalent attachment to RO His and Cys.  The substrate reticuline is seen in the active site cavity interacting with FAD and numerous RO sidechains<ref>PMID:18953357</ref>.
+<scene name='87/873795/Cv/2'>The 3D structure of the complex between three Rab C2B domains and a 4-helix bundle belonging to 4 SNAP-25 monomers</scene>. Two different <scene name='87/873795/Cv/6'>helix-helix interactions between Rab and SNAP-25</scene> are seen. One involves 2 monomers of SNAP-25 and the other involves one monomer<ref>PMID:28634303</ref>. Rab chain A interacts only with SNAP-25 chain D, while Rab chain B interacts with 2 SNAP-25 chains D (residues that interact with Rab chain B are colored salmon) and F.
 </StructureSection>
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 Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-[[2cm5]], [[2cm6]] – rRab C2B domain 541-680 – rat<br />
+Domains: C2A 378-510; C2B 541-680
-[[4izk]] – rRab C2B domain - NMR<br />
+[[2cm5]], [[2cm6]] – rRab C2B domain – rat<br />
+[[3rpb]], [[4izk]] – rRab C2B domain - NMR<br />
 [[5lo8]] – rRab C2B domain + inositol phosphate derivative<br />
-[[5lob]], [[5low]] – rRab C2AB domain + SNAP25<br />
+[[5lob]], [[5low]] – rRab C2B domain + SNAP25<br />
-[[2chd]], [[4lt7]] – rRab C2A domain 378-510 <br />
+[[2chd]], [[4lt7]] – rRab C2A domain <br />
 [[4np9]], [[4ns0]] – rRab C2A domain + inositol phosphate derivative<br />
 [[1zbd]] – rRab 19-217 (mutant) + rRab effector domain 40-179 (mutant) + GTP<br />
-[[2k3h]] – mRab C2A domain 378-510 - mouse - NMR<br />
+[[2k3h]] – mRab C2A domain - mouse - NMR<br />
 == References ==