PDBsum entry 2bkf

Zinc-finger protein

PDB id: 2bkf

Contents

Protein chain

86 a.a.

Ligands

GOL ×2

Waters ×94

PDB id:

2bkf

Name:

Zinc-finger protein

Title:

Structure of the pb1 domain of nbr1

Structure:

Zinc-finger protein nbr1 (next to breast cancer 1). Chain: a. Fragment: residues 1-85 (pb1 interaction domain). Synonym: pb1 domain of nbr1, next to brca1 gene 1 protein, 1a1-3b. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.56Å R-factor: 0.200 R-free: 0.226

Authors:

S.Mueller,I.Kursula,M.Wilmanns

Key ref:

S.Müller et al. (2006). Crystal structure of the PB1 domain of NBR1. FEBS Lett, 580, 341-344. PubMed id: 16376336 DOI: 10.1016/j.febslet.2005.12.021

Date:

16-Feb-05 Release date: 18-Jan-06

Protein chain

Q14596  (NBR1_HUMAN) -  Next to BRCA1 gene 1 protein from Homo sapiens

Seq: 966 a.a.

Struc: 86 a.a.

DOI no: 10.1016/j.febslet.2005.12.021

FEBS Lett 580:341-344 (2006)

PubMed id: 16376336

Crystal structure of the PB1 domain of NBR1.

S.Müller, I.Kursula, P.Zou, M.Wilmanns.

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.

Selected figure(s)

Figure 1.
Fig. 1. Overall structure of the PB1 domain of NBR1 (1–85). (A) Ribbon representation. The type-A PB1 domain residues Asp-50, Glu-52, Glu-54, and Glu-63 are shown in ball-and-stick representation; (B) Electrostatic potential surface of the NBR1 PB1 domain; red indicates negatively charged surface areas and blue indicates positively charged surface areas. The acidic cluster A1 is comprised of Asp50, Glu52, and Glu54; A2 is comprised of Asp63.

Figure 3.
Fig. 3. Model of the TK/NBR1/P62 interaction. The domains with available high resolution structures are shown as ribbons, the remaining domains are shown schematically. The ribbon of titin kinase has been created from the PDB entry 1TK1 [18]. The sequence segments suggested to be involved in the interaction of the p62/NBR1 and NBR1/titin kinase haven been taken from [9] and [10], respectively. To date, there is no detailed analysis available, mapping homo association sites in NBR1. We hypothesise an interaction via the central coiled-coil regions. The first helix of the autoregulatory segment of titin kinase that is involved in the interaction with NBR1 [10] is shown in red. Please note that there is no experimental structure of the ‘kin3’ conformation of titin kinase [10] yet. The N-terminal sequence of titin is indicated by a dashed line, reflecting the giant length of the sequence.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2006, 580, 341-344) copyright 2006.

Figures were selected by an automated process.