1rh8
From Proteopedia
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| - | [[Image:1rh8.jpg|left|200px]] | + | [[Image:1rh8.jpg|left|200px]] |
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| - | '''Three-dimensional structure of the calcium-free Piccolo C2A-domain''' | + | {{Structure |
| + | |PDB= 1rh8 |SIZE=350|CAPTION= <scene name='initialview01'>1rh8</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= PCLO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | }} | ||
| + | |||
| + | '''Three-dimensional structure of the calcium-free Piccolo C2A-domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RH8 is a [ | + | 1RH8 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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14718922 14718922] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:51:41 2008'' |
Revision as of 11:51, 20 March 2008
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| Gene: | PCLO (Rattus norvegicus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1RH8 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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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