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Crystal structure of NMC-4 fab anti-von Willebrand factor A1 domain

Academic Article
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Overview

authors

  • Celikel, R.
  • Madhusudan
  • Varughese, K.
  • Shima, M.
  • Yoshioka, A.
  • Ware, J.
  • Ruggeri, Zaverio

publication date

  • April 1997

journal

  • Blood Cells Molecules and Diseases  Journal

abstract

  • 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.

subject areas

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal
  • Base Sequence
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Immunoglobulin Fab Fragments
  • Immunoglobulin Heavy Chains
  • Immunoglobulin Light Chains
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Recombinant Proteins
  • von Willebrand Factor
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Research

keywords

  • A1 domain
  • Fab structure
  • adhesion
  • aggregation
  • hemostasis
  • platelet
  • thrombosis
  • von Willebrand factor
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Identity

International Standard Serial Number (ISSN)

  • 1079-9796

Digital Object Identifier (DOI)

  • 10.1006/bcmd.1997.0128

PubMed ID

  • 9215757
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Additional Document Info

start page

  • 123

end page

  • 134

volume

  • 23

issue

  • 7

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