4lt7: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lt7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LT7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4lt7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LT7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4lt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lt7 OCA], [https://pdbe.org/4lt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lt7 RCSB], [https://www.ebi.ac.uk/pdbsum/4lt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lt7 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=4lt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lt7 OCA], [https://pdbe.org/4lt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lt7 RCSB], [https://www.ebi.ac.uk/pdbsum/4lt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lt7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 19:25, 20 September 2023
Crystal structure of the c2a domain of rabphilin-3a in complex with a calciumCrystal structure of the c2a domain of rabphilin-3a in complex with a calcium
Structural highlights
FunctionRP3A_RAT Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. Publication Abstract from PubMedProteins containing C2 domains are the sensors for Ca(2+) and PI(4,5)P2 in a myriad of secretory pathways. Here, the use of a free-mounting system has enabled us to capture an intermediate state of Ca(2+) binding to the C2A domain of rabphilin 3A that suggests a different mechanism of ion interaction. We have also determined the structure of this domain in complex with PI(4,5)P2 and IP3 at resolutions of 1.75 and 1.9 A, respectively, unveiling that the polybasic cluster formed by strands beta3-beta4 is involved in the interaction with the phosphoinositides. A comparative study demonstrates that the C2A domain is highly specific for PI(4,5)P2/PI(3,4,5)P3, whereas the C2B domain cannot discriminate among any of the diphosphorylated forms. Structural comparisons between C2A domains of rabphilin 3A and synaptotagmin 1 indicated the presence of a key glutamic residue in the polybasic cluster of synaptotagmin 1 that abolishes the interaction with PI(4,5)P2. Together, these results provide a structural explanation for the ability of different C2 domains to pull plasma and vesicle membranes close together in a Ca(2+)-dependent manner and reveal how this family of proteins can use subtle structural changes to modulate their sensitivity and specificity to various cellular signals. Structural insights into the Ca2+ and PI(4,5)P2 binding modes of the C2 domains of rabphilin 3A and synaptotagmin 1.,Guillen J, Ferrer-Orta C, Buxaderas M, Perez-Sanchez D, Guerrero-Valero M, Luengo-Gil G, Pous J, Guerra P, Gomez-Fernandez JC, Verdaguer N, Corbalan-Garcia S Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):20503-8. doi:, 10.1073/pnas.1316179110. Epub 2013 Dec 3. PMID:24302762[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||