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PDBsum entry 1tnn
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Muscle protein
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PDB id
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1tnn
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References listed in PDB file
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Key reference
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Title
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Tertiary structure of an immunoglobulin-Like domain from the giant muscle protein titin: a new member of the i set.
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Authors
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M.Pfuhl,
A.Pastore.
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Ref.
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Structure, 1995,
3,
391-401.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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BACKGROUND: Titin is a gigantic protein located in the thick filament of
vertebrate muscles. The putative functions of titin range from interactions with
myosin and other muscle proteins to a role in muscle recoil. Analysis of its
complete sequence has shown that titin is a multi-domain protein containing
several copies of modules of 100 amino acids each. These are thought to belong
to the fibronectin type-III and immunoglobulin superfamilies. So far, a complete
structural determination has not been carried out on any of the titin modules.
RESULTS: The three-dimensional structure of an immunoglobulin module, located in
the M-line of the sarcomere close to the titin C terminus and called 'M5', was
determined by multi-dimensional NMR spectroscopy. The structure has the
predicted immunoglobulin fold with two beta-sheets packed against each other.
Each sheet contains four strands. The structure of M5 belongs to the I
(intermediate) set of the immunoglobulin superfamily and is very similar to
telokin, which is also found in muscles. Although M5 and telokin have relatively
little sequence similarity, the two proteins clearly share the same hydrophobic
core. The major difference between telokin and the titin M5 module is the
absence of the C' strand in the latter. CONCLUSIONS: The titin domains and
several of the immunoglobulin-like domains from other modular muscle proteins
are highly conserved at the positions corresponding to the hydrophobic core of
M5. Our results indicate that it may be possible to use the structure of M5 as a
molecular template to model most of the other immunoglobulin-like domains in
muscle titin.
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Figure 7.
Figure 7. Part of the hydrophobic core of M5. A hydrogen bond
is formed between the Tyr70 hydroxyl proton and the backbone
carbonyls of Asp66 and Glu67. The aromatic ring packs against
Leu40. The side chain carboxylate group of Asp66 forms ion
bridges with His46 and weakly with Arg45. Hydrogen bonds/ionic
interactions are indicated by dashed lines. Figure 7. Part of
the hydrophobic core of M5. A hydrogen bond is formed between
the Tyr70 hydroxyl proton and the backbone carbonyls of Asp66
and Glu67. The aromatic ring packs against Leu40. The side chain
carboxylate group of Asp66 forms ion bridges with His46 and
weakly with Arg45. Hydrogen bonds/ionic interactions are
indicated by dashed lines.
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Figure 8.
Figure 8. (a) Interaction of Tyr53 with the loop around
Pro27-Pro29. The aromatic ring of Tyr53 packs against the
hydrophobic surface provided by Pro27, Val28 and Pro29. The two
prolines are in cis and trans conformations, respectively. A
hydrogen bond is formed from the hydroxyl proton of Tyr53 to the
side chain carboxylate of Asp24.(b) Alternative interactions of
Asp24 with Arg1 in the family of 16 accepted structures. Side
chains of Arg1, Asp24 and Tyr53 are shown for the 16 best
structures while the backbone is only shown for the average
structure. Figure 8. (a) Interaction of Tyr53 with the loop
around Pro27-Pro29. The aromatic ring of Tyr53 packs against the
hydrophobic surface provided by Pro27, Val28 and Pro29. The two
prolines are in cis and trans conformations, respectively. A
hydrogen bond is formed from the hydroxyl proton of Tyr53 to the
side chain carboxylate of Asp24. (b) Alternative interactions of
Asp24 with Arg1 in the family of 16 accepted structures. Side
chains of Arg1, Asp24 and Tyr53 are shown for the 16 best
structures while the backbone is only shown for the average
structure.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(1995,
3,
391-401)
copyright 1995.
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Secondary reference #1
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Title
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Secondary structure determination by nmr spectroscopy of an immunoglobulin-Like domain from the giant muscle protein titin.
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Authors
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M.Pfuhl,
M.Gautel,
A.S.Politou,
C.Joseph,
A.Pastore.
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Ref.
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J Biomol Nmr, 1995,
6,
48-58.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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