2K0B

NMR structure of the UBA domain of p62 (SQSTM1)

2K0B の概要

• エントリーDOI: 10.2210/pdb2k0b/pdb
• NMR情報: BMRB: 15591
• 分子名称: Sequestosome-1 (1 entity in total)
• 機能のキーワード: ubiquitin binding, helical bundle, three helices, alternative splicing, apoptosis, cytoplasm, differentiation, disease mutation, endosome, immune response, metal-binding, nucleus, phosphoprotein, polymorphism, zinc, zinc-finger, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q13501
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5744.41

構造登録者

Long, J.E.,Ciani, B.,Gallagher, T.R.A.,Cavey, J.R.,Sheppard, P.W.,Layfield, R.,Searle, M.S. (登録日: 2008-01-31, 公開日: 2008-02-19, 最終更新日: 2024-05-29)

主引用文献

Evans, C.L.,Long, J.E.,Gallagher, T.R.,Hirst, J.D.,Searle, M.S.
Conformation and dynamics of the three-helix bundle UBA domain of p62 from experiment and simulation.
Proteins, 71:227-240, 2007

PubMed Abstract: The ubiquitin associated domain of p62 is a small three-helix bundle of approximately 50 residues that mediates the recognition of polyubiquitin chains and ubiquitylated substrates. The solution structure of a 52 residue construct containing this domain has been characterized using heteronuclear nuclear magnetic resonance (NMR) methods. The resulting ensemble of NMR-derived structures was used in molecular dynamics (MD) simulations to investigate the equilibrium conformation and dynamics of this domain. NOE and (15)N relaxation data have been used to validate the structural ensemble produced by the MD simulations and show a good correlation for residues in regions of secondary structure. A similar approach was taken using an ensemble of structures from the MD simulations to calculate electronic circular dichroism (CD) and IR spectra from first principles with an encouraging correlation with the experimental CD and IR data.

PubMed: 17932931
DOI: 10.1002/prot.21692

実験手法

SOLUTION NMR