The Three-Dimensional Structure of the Fab′ Fragment of a Human Myeloma Immunoglobulin at 2.0-Å Resolution

DOI Web Site 1 Citations
  • R. J. Poljak
    Department of Biophysics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
  • L. M. Amzel
    Department of Biophysics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
  • B. L. Chen
    Department of Biophysics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
  • R. P. Phizackerley
    Department of Biophysics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
  • F. Saul
    Department of Biophysics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Description

<jats:p>The structural analysis of the Fab′ fragment of human myeloma immunoglobulin IgGl(λ) New has been extended to a nominal resolution of 2.0 Å. Each of the structural subunits corresponding to the variable and to the constant homology regions of the light and heavy chains contains two irregular β-sheets which are roughly parallel to each other and surround a tightly packed interior of hydrophobic side chains. About 50-60% of the amino-acid residues are included in β-pleated sheets. Sequence alignments between the homology regions of Fab′ New obtained by comparison of their three-dimensional structures are given. Some of the sequence variations observed in light and heavy chains and the role of the regions of hypervariable sequence in defining the size and shape of the active site of different immunoglobulin molecules are discussed on the basis of the three-dimensional model of Fab′ New.</jats:p>

Journal

Citations (1)*help

See more

Details 詳細情報について

Report a problem

Back to top