[A new crystal form of the Fab fragment of a monoclonal antibody to human interleukin-2: the three-dimensional structure at 2.7 A resolution]
Autor: | I. N. Tsygannik, S. V. Pletnev, Walter Pangborn, W Daux, E A Goriacheva, Vladimir Z. Pletnev, Nesmeianov Va |
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Rok vydání: | 2004 |
Předmět: |
Models
Molecular medicine.drug_class Stereochemistry Protein Conformation Monoclonal antibody Crystallography X-Ray Biochemistry Immunoglobulin Fab Fragments Protein structure medicine Bioorganic chemistry Humans Molecular replacement Antigens biology Chemistry Fragment (computer graphics) Organic Chemistry Resolution (electron density) Antibodies Monoclonal Water Crystallography biology.protein Interleukin-2 Protein folding Antibody |
Zdroj: | Bioorganicheskaia khimiia. 30(5) |
ISSN: | 0132-3423 |
Popis: | The three-dimensional structure of the antigen-binding fragment of a monoclonal antibody to human interleukin-2 in a new crystal form (space group P2(1)2(1)2(1); unit cell parameters: a = 42.82, b = 90.68, and c = 139.82 A) was determined by the X-ray molecular replacement method at the resolution of 2.7 A. The protein folding and the stereochemistry of its antigen-binding site were comparatively analyzed. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 5; see also http: // www.maik.ru. |
Databáze: | OpenAIRE |
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