1rh8: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE= PCLO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
|GENE= PCLO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<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.ebi.ac.uk/pdbsum/1rh8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rh8 RCSB]</span>
}}
}}


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[[Category: beta-sandwich]]
[[Category: beta-sandwich]]


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Revision as of 23:28, 30 March 2008

File:1rh8.jpg


PDB ID 1rh8

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Gene: PCLO (Rattus norvegicus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Three-dimensional structure of the calcium-free Piccolo C2A-domain


OverviewOverview

C2 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.

About this StructureAbout this Structure

1RH8 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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

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