2BKF
Structure of the PB1 domain of NBR1
Summary for 2BKF
Entry DOI | 10.2210/pdb2bkf/pdb |
Related | 1WJ6 2CP8 |
Descriptor | ZINC-FINGER PROTEIN NBR1 (NEXT TO BREAST CANCER 1), GLYCEROL (3 entities in total) |
Functional Keywords | zinc-finger protein, pb1 domain, nbr1, interaction domain, zinc-finger |
Biological source | HOMO SAPIENS (HUMAN) |
Total number of polymer chains | 1 |
Total formula weight | 10055.09 |
Authors | Mueller, S.,Kursula, I.,Wilmanns, M. (deposition date: 2005-02-16, release date: 2006-01-18, Last modification date: 2024-05-08) |
Primary citation | Mueller, 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: 16376336DOI: 10.1016/J.FEBSLET.2005.12.021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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