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Immunoglobulin G1 Fc domain motions: implications for Fc engineering.

Abstract：

:The fragment crystallizable (Fc) region links the key pathogen identification and destruction properties of immunoglobulin G (IgG). Pathogen opsonization positions Fcs to activate pro-inflammatory Fcγ receptors (FcγRs) on immune cells. The cellular response and committal to a damaging, though protective, immune response are tightly controlled at multiple levels. Control mechanisms are diverse and in many cases unclear, but one frequently suggested contribution originates in FcγR affinity being modulated through shifts in Fc conformational sampling. Here, we report a previously unseen IgG1 Fc conformation. This observation motivated an extensive molecular dynamics investigation of polypeptide and glycan motions that revealed greater amplitude of motion for the N-terminal Cγ2 domains and N-glycan than previously observed. Residues in the Cγ2/Cγ3 interface and disulfide-bonded hinge were identified as influencing the Cγ2 motion. Our results are consistent with a model of Fc that is structurally dynamic. Conformational states that are competent to bind immune-stimulating FcγRs interconverted with Fc conformations distinct from those observed in FcγR complexes, which may represent a transient, nonbinding population.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Frank M,Walker RC,Lanzilotta WN,Prestegard JH,Barb AW

doi

10.1016/j.jmb.2014.01.011

subject

Has Abstract

pub_date

2014-04-17 00:00:00

pages

1799-811

issue

8

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(14)00069-2

journal_volume

426

pub_type

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