The three-dimensional structure of the fab' fragment of a human myeloma immunoglobulin at 2.0-angstrom resolution.

Abstract:

:The structural analysis of the Fab' fragment of human myeloma immunoglobulin IgGl(lambda) New has been extended to a nominal resolution of 2.0 A. Each of the structural subunits corresponding to the variable and to the constant homology regions of the light and heavy chains contains two irregular beta-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 beta-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.

authors

Poljak RJ,Amzel LM,Chen BL,Phizackerley RP,Saul F

doi

10.1073/pnas.71.9.3440

subject

Has Abstract

pub_date

1974-09-01 00:00:00

pages

3440-4

issue

9

eissn

0027-8424

issn

1091-6490

journal_volume

71

pub_type

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