Crystal Structure of the RIM1 C2B Domain at 1.7 Å Resolution
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- 作者：Rong Guan ; Han Dai ; Diana R. Tomchick ; Irina Dulubova ; Mischa Machius ; Thomas C. Sü ; dhof ; Josep Rizo
- 刊名：Biochemistry
- 出版年：2007
- 出版时间：August 7, 2007
- 年：2007
- 卷：46
- 期：31
- 页码：8988 - 8998
- 全文大小：916K
- 年卷期：v.46,no.31(August 7, 2007)
- ISSN：1520-4995
文摘
RIM proteins play critical roles in synaptic vesicle priming and diverse forms of presynapticplasticity. The C-terminal C2B domain is the only module that is common to all RIMs but is only distantlyrelated to well-studied C2 domains, and its three-dimensional structure and interactions have not beencharacterized in detail. Using NMR spectroscopy, we now show that N- and C-terminal extensions beyondthe predicted C2B domain core sequence are necessary to form a folded, stable RIM1
rs/alpha.gif" BORDER=0> C2B domain. Wealso find that the isolated RIM1rs/alpha.gif" BORDER=0> C2B domain is not sufficient for previously described protein-proteininteractions involving the RIM1rs/alpha.gif" BORDER=0> C-terminus, suggesting that additional sequences adjacent to the C2Bdomain might be required for these interactions. However, analytical ultracentrifugation shows that theRIM1rs/alpha.gif" BORDER=0> C2B domain forms weak dimers in solution. The crystal structure of the RIM1rs/alpha.gif" BORDER=0> C2B domaindimer at 1.7 Å resolution reveals that it forms a rs/beta2.gif" BORDER=0 ALIGN="middle">-sandwich characteristic of C2 domains and that theunique N- and C-terminal extensions form a small subdomain that packs against the rs/beta2.gif" BORDER=0 ALIGN="middle">-sandwich andmediates dimerization. Our results provide a structural basis to understand the function of RIM C2B domainsand suggest that dimerization may be a crucial aspect of RIM function.
rs/alpha.gif" BORDER=0> C2B domain. Wealso find that the isolated RIM1rs/alpha.gif" BORDER=0> C2B domain is not sufficient for previously described protein-proteininteractions involving the RIM1rs/alpha.gif" BORDER=0> C-terminus, suggesting that additional sequences adjacent to the C2Bdomain might be required for these interactions. However, analytical ultracentrifugation shows that theRIM1rs/alpha.gif" BORDER=0> C2B domain forms weak dimers in solution. The crystal structure of the RIM1rs/alpha.gif" BORDER=0> C2B domaindimer at 1.7 Å resolution reveals that it forms a rs/beta2.gif" BORDER=0 ALIGN="middle">-sandwich characteristic of C2 domains and that theunique N- and C-terminal extensions form a small subdomain that packs against the rs/beta2.gif" BORDER=0 ALIGN="middle">-sandwich andmediates dimerization. Our results provide a structural basis to understand the function of RIM C2B domainsand suggest that dimerization may be a crucial aspect of RIM function.