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Journal ArticleDOI

Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1.

TLDR
Structural insight into the mechanisms of affinity enhancement suggest that the glycoform-dependent ADCC enhancement is attributed to a subtle conformational alteration in a limited region of IgG1-Fc.
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This article is published in Journal of Molecular Biology.The article was published on 2007-05-04. It has received 267 citations till now.

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Journal ArticleDOI

Fcγ receptors as regulators of immune responses

TL;DR: Recent studies addressing the multifaceted roles of FcRs for IgG (FcγRs) in the immune system are discussed and how this knowledge could be translated into novel therapeutic strategies to treat human autoimmune, infectious or malignant diseases are discussed.
Journal ArticleDOI

Glycosylation as a strategy to improve antibody-based therapeutics

TL;DR: Current knowledge of methods and avenues for their exploitation in the clinic are summarized, which allow the production of rMAbs bearing pre-selected oligosaccharides — glycoforms — to provide maximum efficacy for a given disease indication.
Journal ArticleDOI

Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose

TL;DR: A detailed, molecular understanding of the regulatory role of Fc-oligosaccharide core fucosylation in improving ADCC is obtained and a unique mechanism by which the immune system can regulate antibody-mediated effector functions is suggested.
Journal ArticleDOI

Terminal sugars of Fc glycans influence antibody effector functions of IgGs.

TL;DR: Structural studies indicate that the presence or absence of specific terminal sugars may affect hydrophilic and hydrophobic interactions between sugar residues and amino acid residues in the Fc fragment, which in turn may impact antibody effector functions.
Journal ArticleDOI

FcγRIIB in autoimmunity and infection: evolutionary and therapeutic implications

TL;DR: Increased understanding of the function of FcγRIIB has potentially far-reaching therapeutic implications, being involved in the mechanism of action of intravenous immunoglobulin, controlling the efficacy of monoclonal antibody therapy and providing a direct therapeutic target.
References
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Journal ArticleDOI

The Protein Data Bank

TL;DR: The goals of the PDB are described, the systems in place for data deposition and access, how to obtain further information and plans for the future development of the resource are described.
Journal ArticleDOI

PROCHECK: a program to check the stereochemical quality of protein structures

TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
Journal ArticleDOI

The CCP4 suite: programs for protein crystallography

TL;DR: The CCP4 (Collaborative Computational Project, number 4) program suite is a collection of programs and associated data and subroutine libraries which can be used for macromolecular structure determination by X-ray crystallography.
Journal ArticleDOI

Improved methods for building protein models in electron density maps and the location of errors in these models.

TL;DR: In this paper, the authors describe strategies and tools that help to alleviate this problem and simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.
Journal ArticleDOI

Lack of Fucose on Human IgG1 N-Linked Oligosaccharide Improves Binding to Human FcγRIII and Antibody-dependent Cellular Toxicity

TL;DR: Antibody-dependent cellular cytot toxicity assays using purified peripheral blood monocytes or natural killer cells from several donors showed enhanced cytotoxicity, especially evident at lower antibody concentrations.
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