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PDBsum entry 2dcv
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Antimicrobial protein
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PDB id
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2dcv
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References listed in PDB file
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Key reference
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Title
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The solution structure of horseshoe crab antimicrobial peptide tachystatin b with an inhibitory cystine-Knot motif.
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Authors
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N.Fujitani,
T.Kouno,
T.Nakahara,
K.Takaya,
T.Osaki,
S.Kawabata,
M.Mizuguchi,
T.Aizawa,
M.Demura,
S.Nishimura,
K.Kawano.
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Ref.
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J Pept Sci, 2007,
13,
269-279.
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PubMed id
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Abstract
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Tachystatin B is an antimicrobial and a chitin-binding peptide isolated from the
Japanese horseshoe crab (Tachypleus tridentatus) consisting of two isopeptides
called tachystatin B1 and B2. We have determined their solution structures using
NMR experiments and distance geometry calculations. The 20 best converged
structures of tachystatin B1 and B2 exhibited root mean square deviations of
0.46 and 0.49 A, respectively, for the backbone atoms in Cys(4)-Arg(40). Both
structures have identical conformations, and they contain a short antiparallel
beta-sheet with an inhibitory cystine-knot (ICK) motif that is distributed
widely in the antagonists for voltage-gated ion channels, although tachystatin B
does not have neurotoxic activity. The structural homology search provided
several peptides with structures similar to that of tachystatin B. However, most
of them have the advanced functions such as insecticidal activity, suggesting
that tachystatin B may be a kind of ancestor of antimicrobial peptide in the
molecular evolutionary history. Tachystatin B also displays a significant
structural similarity to tachystatin A, which is member of the tachystatin
family. The structural comparison of both tachystatins indicated that Tyr(14)
and Arg(17) in the long loop between the first and second strands might be the
essential residues for binding to chitin.
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Secondary reference #1
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Title
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Horseshoe crab hemocyte-Derived antimicrobial polypeptides, Tachystatins, With sequence similarity to spider neurotoxins.
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Authors
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T.Osaki,
M.Omotezako,
R.Nagayama,
M.Hirata,
S.Iwanaga,
J.Kasahara,
J.Hattori,
I.Ito,
H.Sugiyama,
S.Kawabata.
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Ref.
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J Biol Chem, 1999,
274,
26172-26178.
[DOI no: ]
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PubMed id
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Figure 7.
Fig. 7. Amino acid sequences of tachystatins. Residues
identified using a gas phase sequencer are indicated by arrows.
T, trypsin-digested peptides; C, chymotrypsin-digested peptides;
D, endoproteinase Asp N-digested peptides; K, lysyl
endopeptidase-digested peptides.
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Figure 10.
Fig. 10.  -Sheet
structural models of the COOH-terminal regions of tachystatins
A, B, and C. Solid/dashed lines indicate side chains pointing
out of/into the plane of the diagram. Basic and hydrophobic
amino acid residues are indicated in double underlines and
single underlines, respectively.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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