2L0P

Solution structure of human apo-S100A1 protein by NMR spectroscopy

2L0P の概要

• エントリーDOI: 10.2210/pdb2l0p/pdb
• 分子名称: S100 calcium binding protein A1 (1 entity in total)
• 機能のキーワード: s100a1, calcium binding protein, ef-hand, s100 family
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21113.57

構造登録者

Nowakowski, M.,Jaremko, L.,Jaremko, M.,Bierzynski, A.,Zhukov, I.,Ejchart, A. (登録日: 2010-07-12, 公開日: 2011-04-20, 最終更新日: 2024-05-01)

主引用文献

Nowakowski, M.,Jaremko, L.,Jaremko, M.,Zhukov, I.,Belczyk, A.,Bierzynski, A.,Ejchart, A.
Solution NMR structure and dynamics of human apo-S100A1 protein.
J.Struct.Biol., 174:391-399, 2011

PubMed Abstract: S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most of other members of the S100 protein family, is a multifunctional, regulatory protein involved in a large variety of biological processes and closely associated with several human diseases. The three-dimensional structure of human apo-(i.e. calcium free)-S100A1 protein was determined by NMR spectroscopy (PDB 2L0P) and its backbone dynamics established by ¹⁵N magnetic relaxation. Comparison of these results with the structure and backbone dynamics previously determined for bovine apo-S100A1 protein modified by disulfide formation with β-mercaptoethanol at Cys 85 revealed that the secondary structure of both these proteins was almost identical, whereas the global structure of the latter was much more mobile than that of human apo-S100 protein. Differences between the structures of human and rat apo-S100A1 are also discussed.

PubMed: 21296671
DOI: 10.1016/j.jsb.2011.01.011

実験手法

SOLUTION NMR