Crystallographic structure studies of an IgG molecule and an Fc fragment (Q33853269)

29 July 2017

title

Crystallographic structure studies of an IgG molecule and an Fc fragment (English)

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29 July 2017

Deisenhofer J

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29 July 2017

Huber R

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29 July 2017

Colman PM

series ordinal

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29 July 2017

Matsushima M

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29 July 2017

Palm W

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29 July 2017

language of work or name

English

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publication date

1 December 1976

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29 July 2017

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29 July 2017

volume

264

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29 July 2017

issue

5585

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29 July 2017

page(s)

415-420

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Covalent structure of a human γG-immunoglobulin. VIII. Amino acid sequence of heavy-chain cyanogen bromide fragments H5-H7

29 July 2017

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Three-dimensional structure of immunoglobulins

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Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI.

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Molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution

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Structure of a λ-type Bence-Jones protein at 3.5-Å resolution

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Amino acid sequence of rabbit pneumococcal antibody. I. Light-chain cysteine-containing peptides

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Amino acid sequence of a murine immunoglobulin fragment that possesses complement fixing activity

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The basic trypsin inhibitor of bovine pancreas

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Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution.

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Hinge-regIon deletion localized in the IgG1-globulin Mcg

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Conformational changes induced in a homogeneous antitype III pneumococcal antibody by oligosaccharides of increasing size

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Shape and volume of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as followed by small-angle x-ray scattering

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Shape and volume of fragments Fab' and (Fab')2 of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as determined by small-angle x-ray scattering

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Detection of a conformational change in an antihapten-antibody system upon interaction with divalent hapten

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Kinetic studies on antibody-hapten reactions. I. Reactions with antibodies and their univalent Fab' fragments.

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Structure of the human antibody molecule kol (immunoglobulin G1): An electron density map at 5 Å resolution

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7 January 2021

Crystallographic structural studies of a human Fc-fragment. I. An electron-density map at 4 A resolution and a partial model

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7 January 2021

Crystallographic structural studies of a human Fc fragment. II. A complete model based on a Fourier map at 3.5 A resolution

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7 January 2021

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Tertiary structure of ribonuclease

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The three dimensional structure of a combining region-ligand complex of immunoglobulin NEW at 3.5-A resolution

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The Three-Dimensional Structure of a Phosphorylcholine-Binding Mouse Immunoglobulin Fab and the Nature of the Antigen Binding Site

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Electron microscopy of an antibody-hapten complex.

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Molecular Mechanism of Formation of an Antigen–Antibody Complex

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Segmental flexibility in an antibody molecule

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A search for conformational change on ligand binding in a human M macroglobulin. I. Circular dichroism and hydrogen exchange

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7 January 2021

A search for conformational change on ligand binding in a human M macroglobulin. II. Susceptibility to proteolysis

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7 January 2021

Antigen-induced conformational changes in antibodies and their Fab fragments studied by circular polarization of fluorescence

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Increase of the rotational relaxation time of antibody molecule after complex formation with dansyl-hapten

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7 January 2021

Hapten stabilization of antibody conformation

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7 January 2021

Fluorescence polarization and intensity kinetic studies of antifluorescein antibody obtained at different stages of the immune response

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7 January 2021

Properties of univalent fragments of rabbit antibody isolated by specific adsorption

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7 January 2021

Activation of antibody Fc function by antigen-induced conformational changes

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7 January 2021

Crystallographic Studies of an IgG Immunoglobulin and the Bence-Jones Protein from One Patient

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7 January 2021

Identifiers

DOI

10.1038/264415A0

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Dimensions Publication ID

29 July 2017

1026605089

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