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PDBsum entry 2bkf
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Zinc-finger protein
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PDB id
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2bkf
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the pb1 domain of nbr1.
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Authors
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S.Müller,
I.Kursula,
P.Zou,
M.Wilmanns.
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Ref.
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FEBS Lett, 2006,
580,
341-344.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2006,
580,
341-344)
copyright 2006.
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