1rh8: Difference between revisions
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==Three-dimensional structure of the calcium-free Piccolo C2A-domain== | ==Three-dimensional structure of the calcium-free Piccolo C2A-domain== | ||
<StructureSection load='1rh8' size='340' side='right'caption='[[1rh8 | <StructureSection load='1rh8' size='340' side='right'caption='[[1rh8]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1rh8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1rh8]] is a 1 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=1RH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RH8 FirstGlance]. <br> | ||
</td></tr><tr id=' | </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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh8 OCA], [https://pdbe.org/1rh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh8 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PCLO_RAT PCLO_RAT] May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking (By similarity).[UniProtKB:Q9QYX7] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Garcia | [[Category: Rattus norvegicus]] | ||
[[Category: Gerber | [[Category: Garcia J]] | ||
[[Category: Rizo | [[Category: Gerber SH]] | ||
[[Category: Sudhof | [[Category: Rizo J]] | ||
[[Category: Sugita | [[Category: Sudhof TC]] | ||
[[Category: Sugita S]] | |||
Latest revision as of 12:04, 22 May 2024
Three-dimensional structure of the calcium-free Piccolo C2A-domainThree-dimensional structure of the calcium-free Piccolo C2A-domain
Structural highlights
FunctionPCLO_RAT May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking (By similarity).[UniProtKB:Q9QYX7] 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 PubMedC2 domains are widespread Ca2+-binding modules. The active zone protein Piccolo (also known as Aczonin) contains an unusual C2A domain that exhibits a low affinity for Ca2+, a Ca2+-induced conformational change and Ca2+-dependent dimerization. We show here that removal of a nine-residue sequence by alternative splicing increases the Ca2+ affinity, abolishes the conformational change and abrogates dimerization of the Piccolo C2A domain. The NMR structure of the Ca2+-free long variant provides a structural basis for these different properties of the two splice forms, showing that the nine-residue sequence forms a beta-strand otherwise occupied by a nonspliced sequence. Consequently, Ca2+-binding to the long Piccolo C2A domain requires a marked rearrangement of secondary structure that cannot occur for the short variant. These results reveal a novel mechanism of action of C2 domains and uncover a structural principle that may underlie the alteration of protein function by short alternatively spliced sequences. A conformational switch in the Piccolo C2A domain regulated by alternative splicing.,Garcia J, Gerber SH, Sugita S, Sudhof TC, Rizo J Nat Struct Mol Biol. 2004 Jan;11(1):45-53. Epub 2003 Dec 29. PMID:14718922[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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