2bkf
From Proteopedia
Structure of the PB1 domain of NBR1
Structural highlights
FunctionNBR1_HUMAN Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets.[1] Publication Abstract from PubMedThe 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. Crystal structure of the PB1 domain of NBR1.,Muller S, Kursula I, Zou P, Wilmanns M FEBS Lett. 2006 Jan 9;580(1):341-4. Epub 2005 Dec 19. PMID:16376336[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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