2K0B

NMR structure of the UBA domain of p62 (SQSTM1)

Summary for 2K0B

• Entry DOI: 10.2210/pdb2k0b/pdb
• NMR Information: BMRB: 15591
• Descriptor: Sequestosome-1 (1 entity in total)
• Functional Keywords: 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
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q13501
• Total number of polymer chains: 1
• Total formula weight: 5744.41

Authors

Long, J.E.,Ciani, B.,Gallagher, T.R.A.,Cavey, J.R.,Sheppard, P.W.,Layfield, R.,Searle, M.S. (deposition date: 2008-01-31, release date: 2008-02-19, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

SOLUTION NMR