Crystal structure of the PB1 domain of NBR1.
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 1.55A 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.
Müller
Simone
S
EMBL-Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
Kursula
Inari
I
Zou
Peijian
P
Wilmanns
Matthias
M
D064211:Connectin; D018360:Crystallography, X-Ray; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D009124:Muscle Proteins / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D011494:Protein Kinases / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology
D064211:Connectin; D047908:Intracellular Signaling Peptides and Proteins; D009124:Muscle Proteins; C549756:NBR1 protein, human; D011506:Proteins; C577285:TTN protein, human; D011494:Protein Kinases