1BVK

HUMANIZED ANTI-LYSOZYME FV COMPLEXED WITH LYSOZYME

Summary for 1BVK

• Entry DOI: 10.2210/pdb1bvk/pdb
• Descriptor: HULYS11, LYSOZYME (3 entities in total)
• Functional Keywords: humanized antibody, antibody complex, fv, anti-lysozyme, complex (humanized antibody-hydrolase), complex (humanized antibody-hydrolase) complex, complex (humanized antibody/hydrolase)
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P00698
• Total number of polymer chains: 6
• Total formula weight: 78331.68

Authors

Holmes, M.A.,Buss, T.N.,Foote, J. (deposition date: 1998-09-16, release date: 1999-02-16, Last modification date: 2024-10-23)

Primary citation

Holmes, M.A.,Buss, T.N.,Foote, J.
Conformational correction mechanisms aiding antigen recognition by a humanized antibody.
J.Exp.Med., 187:479-485, 1998

PubMed Abstract: The crystal structure of the complex between hen egg lysozyme and the Fv fragment of a humanized antilysozyme antibody was determined to 2.7-A resolution. The structure of the antigen combining site in the complex is nearly identical to that of the complexed form of the parent mouse antibody, D1.3. In contrast, the combining sites of the unliganded mouse and humanized antilysozymes show moderate conformational differences. This disparity suggests that a conformational readjustment process linked to antigen binding reverses adverse conformations in the complementarity determining regions that had been introduced by engineering these segments next to human framework regions in the humanized antibody.

PubMed: 9463398
DOI: 10.1084/jem.187.4.479

Experimental method

X-RAY DIFFRACTION (2.7 Å)