Three dimensional structure of the Fab' fragment of a human immunoglobulin at 2.8 Å resolution

R. J. Poljak, Mario L Amzel, H. P. Avey, B. L. Chen, R. P. Phizackerley, F. Saul

Research output: Contribution to journalArticle

Abstract

The structure of the Fab' fragment of a human myeloma immunoglobulin was determined by X ray crystallographic analysis at 2.8 Å resolution. The Fourier map of the electron density was correlated with the aminoacid sequence to obtain a 3 dimensional model. 4 globular subunits, which correspond to the homology regions of the light and heavy chains, are arranged in a tetrahedral configuration. These subunits closely resemble each other, sharing a basic pattern of polypeptide chain folding. In each subunit, long sequences of tightly packed, hydrogen bonded polypeptide chains run parallel to the major axis of the subunit. No helical conformation can be seen. Different patterns of interchain disulfide linkage and unusual intrachain disulfide bonds that have been observed in other immunoglobulins can be explained with this model. The regions of hypervariable sequences in the light and heavy chains occur at one end of the molecule, in close spatial proximity.

Original languageEnglish (US)
JournalProceedings of the National Academy of Sciences of the United States of America
Volume70
Issue number12
DOIs
StatePublished - 1973

Fingerprint

Immunoglobulin Fab Fragments
Disulfides
Immunoglobulins
Light
Peptides
Hydrogen
X-Rays
Electrons
myeloma immunoglobulins

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Three dimensional structure of the Fab' fragment of a human immunoglobulin at 2.8 Å resolution. / Poljak, R. J.; Amzel, Mario L; Avey, H. P.; Chen, B. L.; Phizackerley, R. P.; Saul, F.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 70, No. 12, 1973.

Research output: Contribution to journalArticle

@article{b0e58b3f167f4b47b96c52994708bcea,
title = "Three dimensional structure of the Fab' fragment of a human immunoglobulin at 2.8 {\AA} resolution",
abstract = "The structure of the Fab' fragment of a human myeloma immunoglobulin was determined by X ray crystallographic analysis at 2.8 {\AA} resolution. The Fourier map of the electron density was correlated with the aminoacid sequence to obtain a 3 dimensional model. 4 globular subunits, which correspond to the homology regions of the light and heavy chains, are arranged in a tetrahedral configuration. These subunits closely resemble each other, sharing a basic pattern of polypeptide chain folding. In each subunit, long sequences of tightly packed, hydrogen bonded polypeptide chains run parallel to the major axis of the subunit. No helical conformation can be seen. Different patterns of interchain disulfide linkage and unusual intrachain disulfide bonds that have been observed in other immunoglobulins can be explained with this model. The regions of hypervariable sequences in the light and heavy chains occur at one end of the molecule, in close spatial proximity.",
author = "Poljak, {R. J.} and Amzel, {Mario L} and Avey, {H. P.} and Chen, {B. L.} and Phizackerley, {R. P.} and F. Saul",
year = "1973",
doi = "10.1073/pnas.70.12.3305",
language = "English (US)",
volume = "70",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "12",

}

TY - JOUR

T1 - Three dimensional structure of the Fab' fragment of a human immunoglobulin at 2.8 Å resolution

AU - Poljak, R. J.

AU - Amzel, Mario L

AU - Avey, H. P.

AU - Chen, B. L.

AU - Phizackerley, R. P.

AU - Saul, F.

PY - 1973

Y1 - 1973

N2 - The structure of the Fab' fragment of a human myeloma immunoglobulin was determined by X ray crystallographic analysis at 2.8 Å resolution. The Fourier map of the electron density was correlated with the aminoacid sequence to obtain a 3 dimensional model. 4 globular subunits, which correspond to the homology regions of the light and heavy chains, are arranged in a tetrahedral configuration. These subunits closely resemble each other, sharing a basic pattern of polypeptide chain folding. In each subunit, long sequences of tightly packed, hydrogen bonded polypeptide chains run parallel to the major axis of the subunit. No helical conformation can be seen. Different patterns of interchain disulfide linkage and unusual intrachain disulfide bonds that have been observed in other immunoglobulins can be explained with this model. The regions of hypervariable sequences in the light and heavy chains occur at one end of the molecule, in close spatial proximity.

AB - The structure of the Fab' fragment of a human myeloma immunoglobulin was determined by X ray crystallographic analysis at 2.8 Å resolution. The Fourier map of the electron density was correlated with the aminoacid sequence to obtain a 3 dimensional model. 4 globular subunits, which correspond to the homology regions of the light and heavy chains, are arranged in a tetrahedral configuration. These subunits closely resemble each other, sharing a basic pattern of polypeptide chain folding. In each subunit, long sequences of tightly packed, hydrogen bonded polypeptide chains run parallel to the major axis of the subunit. No helical conformation can be seen. Different patterns of interchain disulfide linkage and unusual intrachain disulfide bonds that have been observed in other immunoglobulins can be explained with this model. The regions of hypervariable sequences in the light and heavy chains occur at one end of the molecule, in close spatial proximity.

UR - http://www.scopus.com/inward/record.url?scp=0015733869&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0015733869&partnerID=8YFLogxK

U2 - 10.1073/pnas.70.12.3305

DO - 10.1073/pnas.70.12.3305

M3 - Article

C2 - 4519624

AN - SCOPUS:0015733869

VL - 70

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 12

ER -