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Title
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Crystal structure of NMC-4 fab anti-von Willebrand factor A1 domain.
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Authors
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R.Celikel,
Madhusudan,
K.I.Varughese,
M.Shima,
A.Yoshioka,
J.Ware,
Z.M.Ruggeri.
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Ref.
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Blood Cells Mol Dis, 1997,
23,
123-134.
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PubMed id
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Abstract
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We have solved the crystal structure of the Fab fragment of NMC-4, a mouse
monoclonal antibody that binds to the A1 domain of von Willebrand factor (vWF).
Two Asp and three Tyr residues in the complementarity determining regions 1 and
3 of the heavy chain exhibited a spatial orientation suggestive of a dominant
role in establishing contact with the antigen. A cluster of Asp and Tyr residues
occurs also in a region of the platelet glycoprotein (GP) Ib alpha amino
terminal domain known to be critically involved in vWF binding. Thus, the
structural information obtained with NMC-4 may prove relevant to understand the
stereochemical bases of the GP Ib alpha-vWF interaction essential for thrombus
formation at sites of vascular lesion.
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