1CNP

THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES

1CNP の概要

• エントリーDOI: 10.2210/pdb1cnp/pdb
• 分子名称: CALCYCLIN (RABBIT, APO) (1 entity in total)
• 機能のキーワード: ef-hand, calcium-binding protein, s-100 protein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Nucleus envelope (By similarity): P30801
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20335.46

構造登録者

Potts, B.C.M.,Smith, J.,Akke, M.,Macke, T.J.,Okazaki, K.,Hidaka, H.,Case, D.A.,Chazin, W.J. (登録日: 1995-08-31, 公開日: 1996-10-14, 最終更新日: 2024-05-22)

主引用文献

Potts, B.C.,Smith, J.,Akke, M.,Macke, T.J.,Okazaki, K.,Hidaka, H.,Case, D.A.,Chazin, W.J.
The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.
Nat.Struct.Biol., 2:790-796, 1995

PubMed Abstract: The S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins.

PubMed: 7552751
DOI: 10.1038/nsb0995-790

実験手法

SOLUTION NMR