2bwq
From Proteopedia
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| - | [[Image:2bwq.gif|left|200px]]<br /><applet load="2bwq" size=" | + | [[Image:2bwq.gif|left|200px]]<br /><applet load="2bwq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bwq, resolution 1.41Å" /> | caption="2bwq, resolution 1.41Å" /> | ||
'''CRYSTAL STRUCTURE OF THE RIM2 C2A-DOMAIN AT 1.4 ANGSTROM RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF THE RIM2 C2A-DOMAIN AT 1.4 ANGSTROM RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BWQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain S'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BWQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+S'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:28:40 2008'' |
Revision as of 08:28, 3 February 2008
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CRYSTAL STRUCTURE OF THE RIM2 C2A-DOMAIN AT 1.4 ANGSTROM RESOLUTION
Overview
RIMs are large proteins that contain two C2-domains and are localized at, presynaptic active zones, where neurotransmitters are released. RIMs play, key roles in synaptic vesicle priming and regulation of presynaptic, plasticity. A mutation in the RIM1 C2A-domain has been implicated in, autosomal dominant cone-rod dystrophy (CORD7). The RIM C2A-domain does not, contain the full complement of aspartate residues that commonly mediate, Ca2+ binding at the top loops of C2-domains, and has been reported to, interact with SNAP-25 and synaptotagmin 1, two proteins from the, Ca2+-dependent membrane fusion machinery. Here we have used NMR, spectroscopy and X-ray crystallography to analyze the structure and, biochemical properties of the RIM2 C2A-domain, which is closely related to, the RIM1 C2A-domain. We find that the RIM2 C2A-domain does not bind Ca2+., Moreover, little binding of the RIM2 C2A-domain to SNAP-25 and to the, C2-domains of synaptotagmin 1 was detected by NMR experiments, suggesting, that as yet unidentified interactions of the RIM C2A-domain mediate its, function. The crystal structure of the RIM2 C2A-domain using data to 1.4 A, resolution reveals a beta-sandwich that resembles those observed for other, C2-domains, but exhibits a unique dipolar distribution of electrostatic, charges whereby one edge of the beta-sandwich is highly positive and the, other edge is highly negative. The location of the mutation site, implicated in CORD7 at the bottom of the domain and the pattern of, sequence conservation suggest that, in contrast to most C2-domains, the, RIM C2A-domains may function through Ca2+-independent interactions, involving their bottom face.
About this Structure
2BWQ is a Single protein structure of sequence from Rattus norvegicus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of the RIM2 C2A-domain at 1.4 A resolution., Dai H, Tomchick DR, Garcia J, Sudhof TC, Machius M, Rizo J, Biochemistry. 2005 Oct 18;44(41):13533-42. PMID:16216076
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