1CMF

NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN

1CMF の概要

• エントリーDOI: 10.2210/pdb1cmf/pdb
• 分子名称: CALMODULIN (VERTEBRATE) (1 entity in total)
• 機能のキーワード: calcium-binding protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cytoplasm: P62157
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8416.20

構造登録者

Finn, B.E.,Evenas, J.,Drakenberg, T.,Waltho, J.P.,Thulin, E.,Forsen, S. (登録日: 1995-07-19, 公開日: 1995-12-07, 最終更新日: 2024-05-22)

主引用文献

Finn, B.E.,Evenas, J.,Drakenberg, T.,Waltho, J.P.,Thulin, E.,Forsen, S.
Calcium-induced structural changes and domain autonomy in calmodulin.
Nat.Struct.Biol., 2:777-783, 1995

PubMed Abstract: We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 A and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.

PubMed: 7552749
DOI: 10.1038/nsb0995-777

実験手法

SOLUTION NMR