1RH8

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

1RH8 の概要

• エントリーDOI: 10.2210/pdb1rh8/pdb
• 分子名称: Piccolo protein (1 entity in total)
• 機能のキーワード: beta-sandwich, metal binding protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell junction, synapse: Q9JKS6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16479.60

構造登録者

Garcia, J.,Gerber, S.H.,Sugita, S.,Sudhof, T.C.,Rizo, J. (登録日: 2003-11-14, 公開日: 2004-01-13, 最終更新日: 2024-05-22)

主引用文献

Garcia, J.,Gerber, S.H.,Sugita, S.,Sudhof, T.C.,Rizo, J.
A conformational switch in the Piccolo C2A domain regulated by alternative splicing.
Nat.Struct.Mol.Biol., 11:45-53, 2004

PubMed Abstract: 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.

PubMed: 14718922
DOI: 10.1038/nsmb707

実験手法

SOLUTION NMR