|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution Structure of the RIM1alpha PDZ Domain in Complex with an ELKS1b C-terminal Peptide== | | ==Solution Structure of the RIM1alpha PDZ Domain in Complex with an ELKS1b C-terminal Peptide== |
| - | <StructureSection load='1zub' size='340' side='right'caption='[[1zub]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1zub' size='340' side='right'caption='[[1zub]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zub]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zub]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUB FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rims1, Rim1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Rab6ip2, Cast2, Elks, Erc1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zub OCA], [https://pdbe.org/1zub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zub RCSB], [https://www.ebi.ac.uk/pdbsum/1zub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zub ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zub OCA], [https://pdbe.org/1zub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zub RCSB], [https://www.ebi.ac.uk/pdbsum/1zub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zub ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RIMS1_RAT RIMS1_RAT]] Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity (By similarity). [[https://www.uniprot.org/uniprot/RB6I2_RAT RB6I2_RAT]] Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex (By similarity). May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport.
| + | [https://www.uniprot.org/uniprot/RIMS1_RAT RIMS1_RAT] Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, H]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Lu, J]] | + | [[Category: Li H]] |
| - | [[Category: Rizo, J]] | + | [[Category: Lu J]] |
| - | [[Category: Sudhof, T C]] | + | [[Category: Rizo J]] |
| - | [[Category: Wang, Y]] | + | [[Category: Sudhof TC]] |
| - | [[Category: Complex]]
| + | [[Category: Wang Y]] |
| - | [[Category: Endocytosis-exocytosis complex]]
| + | |
| - | [[Category: Pdz domain]]
| + | |
| Structural highlights
Function
RIMS1_RAT Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
PDZ domains are widespread protein modules that commonly recognize C-terminal sequences of target proteins and help to organize macromolecular signaling complexes. These sequences usually bind in an extended conformation to relatively shallow grooves formed between a beta-strand and an alpha-helix in the corresponding PDZ domains. Because of this binding mode, many PDZ domains recognize primarily the C-terminal and the antepenultimate side-chains of the target protein, which commonly conform to motifs that have been categorized into different classes. However, an increasing number of PDZ domains have been found to exhibit unusual specificities. These include the PDZ domain of RIMs, which are large multidomain proteins that regulate neurotransmitter release and help to organize presynaptic active zones. The RIM PDZ domain binds to the C-terminal sequence of ELKS with a unique specificity that involves each of the four ELKS C-terminal residues. To elucidate the structural basis for this specificity, we have determined the 3D structure in solution of an RIM/ELKS C-terminal peptide complex using NMR spectroscopy. The structure shows that the RIM PDZ domain contains an unusually deep and narrow peptide-binding groove with an exquisite shape complementarity to the four ELKS C-terminal residues in their bound conformation. This groove is formed, in part, by a set of side-chains that is conserved selectively in RIM PDZ domains and that hence determines, at least in part, their unique specificity.
Solution structure of the RIM1alpha PDZ domain in complex with an ELKS1b C-terminal peptide.,Lu J, Li H, Wang Y, Sudhof TC, Rizo J J Mol Biol. 2005 Sep 16;352(2):455-66. PMID:16095618[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu J, Li H, Wang Y, Sudhof TC, Rizo J. Solution structure of the RIM1alpha PDZ domain in complex with an ELKS1b C-terminal peptide. J Mol Biol. 2005 Sep 16;352(2):455-66. PMID:16095618 doi:10.1016/j.jmb.2005.07.047
|
