Structural highlights
Function
NBR1_HUMAN Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets.[1]
Publication Abstract from PubMed
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.
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
- ↑ Kirkin V, Lamark T, Sou YS, Bjorkoy G, Nunn JL, Bruun JA, Shvets E, McEwan DG, Clausen TH, Wild P, Bilusic I, Theurillat JP, Overvatn A, Ishii T, Elazar Z, Komatsu M, Dikic I, Johansen T. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol Cell. 2009 Feb 27;33(4):505-16. doi: 10.1016/j.molcel.2009.01.020. PMID:19250911 doi:10.1016/j.molcel.2009.01.020
- ↑ Muller S, Kursula I, Zou P, Wilmanns M. Crystal structure of the PB1 domain of NBR1. FEBS Lett. 2006 Jan 9;580(1):341-4. Epub 2005 Dec 19. PMID:16376336 doi:http://dx.doi.org/S0014-5793(05)01482-1
