1rh8: Difference between revisions

Revision as of 00:01, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rh8.png

Template:STRUCTURE 1rh8

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

Template:ABSTRACT PUBMED 14718922

About this StructureAbout this Structure

1RH8 is a Single protein structure of sequence from Rattus norvegicus. Full experimental 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Three-dimensional structure of the calcium-free Piccolo C2A-domain'''
+===Three-dimensional structure of the calcium-free Piccolo C2A-domain===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14718922}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14718922 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14718922}}
 ==About this Structure==
-RH8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH8 OCA].
+RH8 is a [[Single protein]] structure of sequence from [http://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].
 ==Reference==
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 [[Category: Sugita, S.]]
 [[Category: Beta-sandwich]]
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