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PDBsum entry 1umr
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Sugar binding protein
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PDB id
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1umr
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Contents |
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* Residue conservation analysis
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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 platelet activator convulxin, A disulfide-Linked alpha4beta4 cyclic tetramer from the venom of crotalus durissus terrificus.
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Authors
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M.T.Murakami,
S.P.Zela,
L.M.Gava,
S.Michelan-Duarte,
A.C.Cintra,
R.K.Arni.
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Ref.
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Biochem Biophys Res Commun, 2003,
310,
478-482.
[DOI no: ]
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PubMed id
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Abstract
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Convulxin (CVX), a C-type lectin, isolated from the venom of the South American
rattlesnake Crotalus durissus terrificus, causes cardiovascular and respiratory
disturbances and is a potent platelet activator which binds to platelet
glycoprotein GPVI. The structure of CVX has been solved at 2.4A resolution to a
crystallographic residual of 18.6% (R(free)=26.4%). CVX is a disulfide linked
heterodimer consisting of homologous alpha and beta chains. The heterodimers are
additionally linked by disulfide bridges to form cyclic
alpha(4)beta(4)heterotetramers. These domains exhibit significant homology to
the carbohydrate-binding domains of C-type lectins, to the factor IX-binding
protein (IX-bp), and to flavocetin-A (Fl-A) but sequence and structural
differences are observed in both the domains in the putative Ca(2+)and
carbohydrate binding regions.
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Secondary reference #1
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Title
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Initial structural analysis of an alpha4beta4 c-Type lectin from the venom of crotalus durissus terrificus.
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Authors
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M.T.Murakami,
L.Watanabe,
L.M.Gava,
S.P.Zela,
A.C.Cintra,
R.K.Arni.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2003,
59,
1813-1815.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Photomicrograph of tetragonal crystals of CVX (maximum
dimension 0.1 mm).
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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