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2BKF

Structure of the PB1 domain of NBR1

Summary for 2BKF
Entry DOI10.2210/pdb2bkf/pdb
Related1WJ6 2CP8
DescriptorZINC-FINGER PROTEIN NBR1 (NEXT TO BREAST CANCER 1), GLYCEROL (3 entities in total)
Functional Keywordszinc-finger protein, pb1 domain, nbr1, interaction domain, zinc-finger
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains1
Total formula weight10055.09
Authors
Mueller, S.,Kursula, I.,Wilmanns, M. (deposition date: 2005-02-16, release date: 2006-01-18, Last modification date: 2024-05-08)
Primary citationMueller, S.,Kursula, I.,Zou, P.,Wilmanns, M.
Crystal Structure of the Pb1 Domain of Nbr1
FEBS Lett., 580:341-, 2006
Cited by
PubMed 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.
PubMed: 16376336
DOI: 10.1016/J.FEBSLET.2005.12.021
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.56 Å)
Structure validation

226707

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