期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 50, 期 1, 页码 153-156出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2011.10.012
关键词
Malaria transmission blocking antibody; 2A8; Crystallization; X-ray structure
资金
- JNU capacity buildup
- JNU UGC networking
- Council of Scientific and Industrial Research (CSIR), India
- Department of Science & Technology (DST), New Delhi, India
- US Department of Energy, Office of Basic Energy Sciences
Understanding the structural basis of recognition between antigen and antibody requires the structural comparison of free and complexed components. Previously, we have reported the crystal structure of the complex between Fab fragment of murine monoclonal antibody 2A8 (Fab2A8) and Plasmodium vivax P25 protein (Pvs25) at 3.2 angstrom resolution. We report here the crystallization and X-ray structure of native Fab2A8 at 4.0 angstrom resolution. The 2A8 antibody generated against Pvs25 prevents the formation of P. vivax oocysts in the mosquito, when assayed in membrane feeding experiment. Comparison of native Fab2A8 structure with antigen bound Fab2A8 structure indicates the significant conformational changes in CDR-H1 and CDR-H3 regions Of V-H domain and CDR-L3 region of V-L domain Of Fab2A8. Upon complex formation, the relative orientation between V-L and V-H domains of Fab2A8 is conserved, while significant differences are observed in elbow angles of heavy and light chains. The combing site residues of complexed Fab2A8 exhibited the reduced temperature factor compared to native Fab2A8, suggesting a loss of conformational entropy upon antigen binding. (C) 2011 Elsevier B.V. All rights reserved.
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