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FEBS Lett. 2006 Jan 9;580(1):341-4. Epub 2005 Dec 19.

Crystal structure of the PB1 domain of NBR1.

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1
EMBL-Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.

Abstract

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.

PMID:
16376336
DOI:
10.1016/j.febslet.2005.12.021
[Indexed for MEDLINE]
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