Crystallization and Preliminary X-Ray Studies of the Fab Fragment from a Humanized Version of the Mouse Anti-Human Fas Antibody Hfe7a

Authors: Ito S.; Takayama T.; Hanzawa H.; Takahashi T.; Miyadai K.; Serizawa N.; Haruyama H.; Hata T.

Source: Protein and Peptide Letters, Volume 9, Number 3, June 2002 , pp. 259-263(5)

Publisher: Bentham Science Publishers

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Abstract:

A humanized version of the apoptosis-inducing mouse anti-human Fas monoclonal antibody, HFE7A, is under further development for the treatment of autoimmune diseases such as rheumatoid arthritis. We have crystallized the antigen-binding fragment (Fab) of the humanized HFE7A. The crystals belong to the orthorhombic space group P2 1 2 1 2 1 with cell dimensions a = 54.4 Å, b = 82.7 Å, c = 104.9 Å and contain one Fab molecule in the asymmetric unit. X-ray diffraction data were collected to 2.8 Å resolution.

Keywords: fab fragment; humanized hfe7a; fas monoclonal antibody

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866023408715

Publication date: 2002-06-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.