Crystal structures of immunoglobulin Fc heterodimers reveal the molecular basis for heterodimer formation

Molecular Immunology

Volumn 65, Issue 2, 2015, Pages 377-383

  Choi, Hye Ji ^a   Seok, Seung Hyeon ^a   Kim, Ye Jin ^a   Seo, Min Duk ^a   Kim, Yong Sung ^a  

^a Ajou University   (South Korea)

Author keywords

Asymmetric disulfide bonds; Bispecific antibody; CH3 domain interface; Fc engineering; Immunoglobulin Fc heterodimer; Thermal stability

Indexed keywords

BISPECIFIC ANTIBODY; HETERODIMER; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; DISULFIDE BOND; GLYCOSYLATION; MOLECULAR INTERACTION; PRIORITY JOURNAL; STATIC ELECTRICITY; STEREOSPECIFICITY; THERMODYNAMICS; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY; CHEMISTRY; HUMAN; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION;

CRYSTALLOGRAPHY, X-RAY; HUMANS; IMMUNOGLOBULIN FC FRAGMENTS; IMMUNOGLOBULIN G; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84923930637     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2015.02.017     Document Type: Article

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