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- Title
Structure of the Janus-faced C<sub>2</sub>B domain of rabphilin.
- Authors
Ubach, Josep; García, Jesús; Nittler, M. Paige; Südhof, Thomas C.; Rizo, Josep
- Abstract
C[SUB2] 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 C[SUB2] domains (C[SUB2]A and C[SUB2]B, respectively) have a high degree of homology but also specific differences. The structure of the C[SUB2]A domain of synaptotagmin I has been extensively studied but little is known about the C[SUB2]B domains. We have used NMR spectroscopy to determine the solution structure of the C[SUB2]B domain of rabphilin. The overall structure of the C[SUB2]B domain is very similar to that of other C[SUB2] domains, with a rigid β-sandwich core and loops at the top (where Ca[SUP2+] binds) and the bottom. Surprisingly, a relatively long α-helix is inserted at the bottom of the domain and is conserved in all C[SUB2]B domains. Our results, together with the Ca[SUP2+]-independent interactions observed for C[SUB2]B domains, indicate that these domains have a Janus-faced nature, with a Ca[SUP2+]-binding top surface and a Ca[SUP+]-independent bottom surface.
- Subjects
PROTEINS; SPECTRUM analysis; HOMOLOGY (Biology)
- Publication
Nature Cell Biology, 1999, Vol 1, Issue 2, p106
- ISSN
1465-7392
- Publication type
Article