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PDBsum entry 1wiu
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Muscle protein
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PDB id
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1wiu
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References listed in PDB file
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Key reference
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Title
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Structure and stability of an immunoglobulin superfamily domain from twitchin, A muscle protein of the nematode caenorhabditis elegans.
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Authors
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S.Fong,
S.J.Hamill,
M.Proctor,
S.M.Freund,
G.M.Benian,
C.Chothia,
M.Bycroft,
J.Clarke.
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Ref.
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J Mol Biol, 1996,
264,
624-639.
[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
percentage match of
96%.
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Abstract
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The NMR solution structure of an immunoglobulin superfamily module of twitchin
(Ig 18') has been determined and the kinetic and equilibrium folding behaviour
characterised. Thirty molecular coordinates were calculated using a hybrid
distance geometry-simulated annealing protocol based on 1207 distance and 48
dihedral restraints. The atomic rms distributions about the mean coordinate for
the ensemble of structures is 0.55( +/- 0.09) A for backbone atoms and 1.10( +/-
0.08) A for all heavy atoms. The protein has a topology very similar to that of
telokin and the titin Ig domains and thus it falls into the I set of the
immunoglobulin superfamily. The close agreement between the predicted and
observed structures of Ig 18' demonstrates clearly that the I set profile can be
applied in the structure prediction of immunoglobulin-like domains of diverse
modular proteins. Folding studies reveal that the protein has relatively low
thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1) at physiological pH.
Unfolding studies suggest that the protein has considerable kinetic stability,
the half life of the unfolding is greater than 40 minutes in the absence of
denaturant.
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Figure 8.
Figure 8. Schematic picture of the three-dimensional
folding topology of Ig 18' generated from the minimized
average structure with the program MolScript (Kraulis,
1991).
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Figure 9.
Figure 9. Stereoview of an overlay of the hydrophobic core residues of telokin, Ig 18', titin M5 and VCAM-d1. The
alignment was a structural alignment based on the I set profile shown below. Colours: telokin, purple (backbone
shown); Ig 18', cyan; titin M5, red; VCAM-d1, green.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1996,
264,
624-639)
copyright 1996.
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Secondary reference #1
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Title
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Additional sequence complexity in the muscle gene, Unc-22, And its encoded protein, Twitchin, Of caenorhabditis elegans.
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Authors
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G.M.Benian,
S.W.L'Hernault,
M.E.Morris.
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Ref.
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Genetics, 1993,
134,
1097-1104.
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PubMed id
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Secondary reference #2
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Title
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Sequence of an unusually large protein implicated in regulation of myosin activity in c. Elegans.
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Authors
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G.M.Benian,
J.E.Kiff,
N.Neckelmann,
D.G.Moerman,
R.H.Waterston.
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Ref.
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Nature, 1989,
342,
45-50.
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PubMed id
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