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Crystal structure of the PB1 domain of NBR1
Author(s) -
Müller Simone,
Kursula Inari,
Zou Peijian,
Wilmanns Matthias
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.021
Subject(s) - titin , scaffold protein , protein kinase domain , microbiology and biotechnology , protein kinase a , biophysics , chemistry , protein structure , signal transducing adaptor protein , biology , signal transduction , kinase , biochemistry , myocyte , sarcomere , gene , mutant
The scaffold protein NBR1 is involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Its N‐terminal Phox and Bem1p (PB1) domain plays a critical role in mediating protein–protein interactions with both titin kinase and with another scaffold protein, p62. We have determined the crystal structure of the PB1 domain of NBR1 at 1.55 Å resolution. It reveals a type‐A PB1 domain with two negatively charged residue clusters. We provide a structural perspective on the involvement of NBR1 in the titin kinase signalling pathway.