1rh8: Difference between revisions
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<StructureSection load='1rh8' size='340' side='right' caption='[[1rh8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1rh8' size='340' side='right' caption='[[1rh8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1rh8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1rh8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RH8 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCLO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCLO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rh8 RCSB], [http://www.ebi.ac.uk/pdbsum/1rh8 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh8 OCA], [http://pdbe.org/1rh8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rh8 RCSB], [http://www.ebi.ac.uk/pdbsum/1rh8 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1rh8" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Buffalo rat]] | ||
[[Category: Garcia, J]] | [[Category: Garcia, J]] | ||
[[Category: Gerber, S H]] | [[Category: Gerber, S H]] | ||
Revision as of 11:54, 10 September 2015
Three-dimensional structure of the calcium-free Piccolo C2A-domainThree-dimensional structure of the calcium-free Piccolo C2A-domain
Structural highlights
Function[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 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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