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

descriptionPublicationkeyboard_double_arrow_right Article 01 Sep 1974Publisher:Proceedings of the National Academy of SciencesJournal:Proceedings of the National Academy of Sciences, volume 71, pages 3,440-3,444 (issn: 0027-8424, eissn: 1091-6490,

Authors: Roberto J. Poljak; B. L. Chen; Frederick Saul; R. P. Phizackerley; L. M. Amzel;

doi: 10.1073/pnas.71.9.3440

pmid: 4215080

pmc: PMC433789

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

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Abstract

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.

Related Organizations

Johns Hopkins University
United States
Johns Hopkins Medicine
United States

Keywords

Models, Molecular, Binding Sites, Fourier Analysis, Protein Conformation, Models, Structural, Immunoglobulin Fab Fragments, Myeloma Proteins, Chromatography, Gel, Humans, Amino Acid Sequence, Immunoglobulin Heavy Chains

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AltName: Full=Ig lambda-3 chain C regions {ECO:0000305};
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