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PDBsum entry 2j8o
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Structural protein
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PDB id
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2j8o
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References listed in PDB file
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Key reference
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Title
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Rigid conformation of an immunoglobulin domain tandem repeat in the a-Band of the elastic muscle protein titin.
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Authors
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S.Müller,
S.Lange,
M.Gautel,
M.Wilmanns.
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Ref.
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J Mol Biol, 2007,
371,
469-480.
[DOI no: ]
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PubMed id
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Abstract
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Most of the structure of the giant muscle protein titin is formed by small
modular domains. Many of them are predicted to be arranged in repeats with short
linkers that may be key determinants of the peculiar elastic properties of
titin. Here, we present the molecular structure of a tandem arrangement of two
immunoglobulin-like domains, A168 and A169, located within the A-band segment of
titin. The two domains are connected by a 17 residue long beta-strand and form a
common interface. Based on these data, we establish general principles to
estimate the amount of conformational flexibility of tandem domain motifs in
titin. An unusual bulge within the second domain, A169, is directly involved
into binding to a sarcomeric ligand, MURF-1, thus suggesting a dual role of this
tandem for both the mechanical properties of titin and for sarcomeric signaling.
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Figure 2.
Figure 2. Schematic presentation of the A168–A169
connecting β-strand (blue) and interacting β-strands from IG
β-sheets. The β-strand residues are colored according to the
scheme used in Figure 6, highlighting whether they belong to the
first or the second I-set IG β-sheet. The background colors of
each β-sheet are adopted from the scheme used in Figure 1,
indicating whether the β-sheet belongs to domain A168 or A169.
Residue numbers are given for the first and last residue of each
β-strand. The β-strand labels are indicated in appropriate
colors above and below the presentation.
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Figure 7.
Figure 7. Model of the domain architecture and ligand
interaction sites from the titin A-band/M-band transition zone.
IG domain tandems, red/dark red; FN-III domains, light brown;
titin kinase, cyan; the interaction sites for several A-band and
kinase downstream ligands^15 are shown schematically, except for
the PB1 domain of NBR1 (green) with an available molecular
structure.^51 The domain nomenclature is indicated on top.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
371,
469-480)
copyright 2007.
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