3RPB
THE C2B-DOMAIN OF RABPHILIN: STRUCTURAL VARIATIONS IN A JANUS-FACED DOMAIN
Summary for 3RPB
| Entry DOI | 10.2210/pdb3rpb/pdb |
| Descriptor | RABPHILIN 3-A (1 entity in total) |
| Functional Keywords | c2-domains, c2b-domain, rabphilin, endocytosis-exocytosis complex, endocytosis/exocytosis |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cell junction, synapse (By similarity): P47709 |
| Total number of polymer chains | 1 |
| Total formula weight | 16253.78 |
| Authors | Ubach, J.,Garcia, J.,Nittler, M.P.,Sudhof, T.C.,Rizo, J. (deposition date: 1999-04-19, release date: 1999-12-23, Last modification date: 2024-05-22) |
| Primary citation | Ubach, J.,Garcia, J.,Nittler, M.P.,Sudhof, T.C.,Rizo, J. Structure of the Janus-faced C2B domain of rabphilin. Nat.Cell Biol., 1:106-112, 1999 Cited by PubMed Abstract: C2 domains are widespread protein modules that often occur as tandem repeats in many membrane-trafficking proteins such as synaptotagmin and rabphilin. The first and second C2 domains (C2A and C2B, respectively) have a high degree of homology but also specific differences. The structure of the C2A domain of synaptotagmin I has been extensively studied but little is known about the C2B domains. We have used NMR spectroscopy to determine the solution structure of the C2B domain of rabphilin. The overall structure of the C2B domain is very similar to that of other C2 domains, with a rigid beta-sandwich core and loops at the top (where Ca2+ binds) and the bottom. Surprisingly, a relatively long alpha-helix is inserted at the bottom of the domain and is conserved in all C2B domains. Our results, together with the Ca(2+)-independent interactions observed for C2B domains, indicate that these domains have a Janus-faced nature, with a Ca(2+)-binding top surface and a Ca(2+)-independent bottom surface. PubMed: 10559882DOI: 10.1038/10076 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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