related to degree

• Saphire, Erica Ollmann, Ph.D., Scripps Research 1994 - 2000

authors

• Saphire, Erica Ollmann
• Stanfield, Robyn
• Crispin, Max
• Parren, P. W. H. I.
• Rudd, P. M.
• Dwek, R. A.
• Burton, Dennis
• Wilson, Ian

publication date

• May 2002

journal

• Journal of Molecular Biology  Journal

abstract

• The crystal structure of IgG1 b12 represents the first visualization of an intact human IgG with a full-length hinge that has all domains ordered and visible. In comparison to intact murine antibodies and hinge-deletant human antibodies, b12 reveals extreme asymmetry, indicative of the extraordinary interdomain flexibility within an antibody. In addition, the structure provides an illustration of the human IgG1 hinge in its entirety and of asymmetry in the composition of the carbohydrate attached to each C(H)2 domain of the Fc. The two separate hinges assume different conformations in order to accommodate the vastly different placements of the two Fab domains relative to the Fc domain. Interestingly, only one of two possible intra-hinge disulfides is formed.

subject areas

• Animals
• Binding Sites, Antibody
• Crystallography, X-Ray
• Disulfides
• Humans
• Immunoglobulin Fab Fragments
• Immunoglobulin Fc Fragments
• Immunoglobulin G
• Mice
• Models, Molecular
• Pliability
• Protein Structure, Tertiary
• Static Electricity
• Structure-Activity Relationship

keywords

• IgG
• antibody structure
• hinge region
• immune recognition
• intact antibody

International Standard Serial Number (ISSN)

• 0022-2836

Digital Object Identifier (DOI)

• 10.1016/s0022-2836(02)00244-9

PubMed ID

• 12051932

start page

• 9

end page

• 18

volume

• 319

issue

• 1