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PDBsum entry 1cdt
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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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Cardiotoxin VII4 from naja mossambica mossambica. The refined crystal structure.
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Authors
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B.Rees,
A.Bilwes,
J.P.Samama,
D.Moras.
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Ref.
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J Mol Biol, 1990,
214,
281-297.
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PubMed id
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Abstract
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The crystal structure of cardiotoxin VII4 from Naja mossambica mossambica was
refined to 2.5 A resolution. Fifty ordered solvent sites were localized and
included in the refinement. The final R factor is 0.197 (lambda/(2sin theta)
less than 5 A; F greater than 3 sigma). The three-dimensional structure is
characterized by two beta-sheets. Of particular interest is the two-stranded
beta-sheet in the N-terminal region. This shows a large right-handed twist and,
though strongly connected to the core of the molecule, and in particular to the
C-terminal end, protrudes out of the bulk of the molecule. The segment of four
amino acid residues connecting the two strands of this sheet is particularly
exposed. It contains an invariant proline residue that has probably an important
structural role, and is completely hydrophobic. Two other conserved hydrophobic
zones were identified; the largest extends over the second and third loops, on
one side only of the molecule. All side-chains of invariant hydrophobic
character (except proline residues) belong to one of these three zones. Also
discussed are the dimeric assembly and the rather loose packing in the crystal.
The three-dimensional structure is compared with that of short and long
alpha-neurotoxins. Comparison with two-dimensional nuclear magnetic resonance
results on the 68% homologous cardiotoxin CT X IIb shows an excellent overall
agreement. A few differences are probably genuine.
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Secondary reference #1
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Title
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Crystal structure of a snake venom cardiotoxin.
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Authors
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B.Rees,
J.P.Samama,
J.C.Thierry,
M.Gilibert,
J.Fischer,
H.Schweitz,
M.Lazdunski,
D.Moras.
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Ref.
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Proc Natl Acad Sci U S A, 1987,
84,
3132-3136.
[DOI no: ]
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PubMed id
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