1rh8
From Proteopedia
(New page: 200px<br /><applet load="1rh8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rh8" /> '''Three-dimensional structure of the calcium-f...) |
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| - | [[Image:1rh8.jpg|left|200px]]<br /><applet load="1rh8" size=" | + | [[Image:1rh8.jpg|left|200px]]<br /><applet load="1rh8" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Three-dimensional structure of the calcium-free Piccolo C2A-domain'''<br /> | '''Three-dimensional structure of the calcium-free Piccolo C2A-domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | C2 domains are widespread Ca2+-binding modules. The active zone protein | + | 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== | ==About this Structure== | ||
| - | 1RH8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1RH8 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Garcia, J.]] | [[Category: Garcia, J.]] | ||
| - | [[Category: Gerber, S | + | [[Category: Gerber, S H.]] |
[[Category: Rizo, J.]] | [[Category: Rizo, J.]] | ||
| - | [[Category: Sudhof, T | + | [[Category: Sudhof, T C.]] |
[[Category: Sugita, S.]] | [[Category: Sugita, S.]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:53 2008'' |
Revision as of 12:50, 21 February 2008
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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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