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PDBsum entry 1tej
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Protein binding
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PDB id
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1tej
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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 disintegrin heterodimer from saw-Scaled viper (echis carinatus) at 1.9 a resolution.
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Authors
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S.Bilgrami,
S.Yadav,
P.Kaur,
S.Sharma,
M.Perbandt,
C.Betzel,
T.P.Singh.
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Ref.
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Biochemistry, 2005,
44,
11058-11066.
[DOI no: ]
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PubMed id
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Abstract
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Disintegrins constitute a family of potent polypeptide inhibitors of integrins.
Integrins are transmembrane heterodimeric molecules involved in cell-cell and
cell-extracellular matrix interactions. They are involved in many diseases such
as cancer and thrombosis. Thus, disintegrins have a great potential as
anticancer and antithrombotic agents. A novel heterodimeric disintegrin was
isolated from the venom of saw-scaled viper (Echis carinatus) and was
crystallized. The crystals diffracted to 1.9 A resolution and belonged to space
group P4(3)2(1)2. The data indicated the presence of a pseudosymmetry. The
structure was solved by applying origin shifts to the disintegrin homodimer
schistatin solved in space group I4(1)22 with similar cell dimensions. The
structure refined to the final R(cryst)/R(free) factors of 0.213/0.253. The
notable differences are observed between the loops, (Gln39-Asp48) containing the
important Arg42-Gly43-Asp44, of the present heterodimer and schistatin. These
differences are presumably due to the presence of two glycines at positions 43
and 46 that allow the molecule to adopt variable conformations. A comparative
analysis of the surface-charge distributions of various disintegrins showed that
the charge distribution on monomeric disintegrins occurred uniformly over the
whole surface of the molecule, while in the dimeric disintegrins, the charge is
distributed only on one face. Such a feature may be important in the binding of
two integrins to a single dimeric disintegrin. The phylogenetic analysis
developed on the basis of amino acid sequence and three-dimensional structures
indicates that the protein diversification and evolution presumably took place
from the medium disintegrins and both the dimeric and short disintegrins evolved
from them.
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