1rh8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1rh8.jpg|left|200px]] | [[Image:1rh8.jpg|left|200px]] | ||
'''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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 20: | Line 29: | ||
[[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 14:51, 20 March 2008
| |||||||
| Gene: | PCLO (Rattus norvegicus) | ||||||
| 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
Page seeded by OCA on Thu Mar 20 13:51:41 2008