1M39

Solution structure of the C-terminal fragment (F86-I165) of the human centrin 2 in calcium saturated form

1M39 の概要

• エントリーDOI: 10.2210/pdb1m39/pdb
• NMR情報: BMRB: 5503
• 分子名称: Caltractin, isoform 1 (1 entity in total)
• 機能のキーワード: ef-hand, cell cycle
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton, centrosome, centriole: P41208
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10390.69

構造登録者

Matei, E.,Miron, S.,Blouquit, Y.,Duchambon, P.,Durussel, P.,Cox, J.A.,Craescu, C.T. (登録日: 2002-06-27, 公開日: 2003-03-25, 最終更新日: 2024-05-22)

主引用文献

Matei, E.,Miron, S.,Blouquit, Y.,Duchambon, P.,Durussel, P.,Cox, J.A.,Craescu, C.T.
C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain
Biochemistry, 42:1439-1450, 2003

PubMed Abstract: Human centrin 2 (HsCen2) is an EF-hand protein that plays a critical role in the centrosome duplication and separation during cell division. We studied the structural and Ca(2+)-binding properties of two C-terminal fragments of this protein: SC-HsCen2 (T94-Y172), covering two EF-hands, and LC-HsCen2 (M84-Y172), having 10 additional residues. Both fragments are highly disordered in the apo state but become better structured (although not conformationally homogeneous) in the presence of Ca(2+) and depending on the nature of the cations (K(+) or Na(+)) in the buffer. Only the longer C-terminal domain, in the Ca(2+)-saturated state and in the presence of Na(+) ions, was amenable to structure determination by nuclear magnetic resonance. The solution structure of LC-HsCen2 reveals an open two EF-hand structure, similar to the conformation of related Ca(2+)-saturated regulatory domains. Unexpectedly, the N-terminal helix segment (F86-T94) lies over the exposed hydrophobic cavity. This unusual intramolecular interaction increases considerably the Ca(2+) affinity and constitutes a useful model for the target binding.

PubMed: 12578356
DOI: 10.1021/bi0269714

実験手法

SOLUTION NMR