Ravishankar, R. ; Ravindran, M. ; Suguna, K. ; Surolia, A. ; Vijayan, M. (1997) Crystal structure of the peanut lectin - T-antigen complex. Carbohydrate specificity generated by water bridges Current Science, 72 (11). pp. 855-861. ISSN 0011-3891
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Official URL: http://www.ias.ac.in/j_archive/currsci/72/11/855-8...
Abstract
Peanut lectin binds with high specificity to the tumour associated disaccharide GaI.81-3GaINAc, generally known as T-antigen. The crystal structure of the complex of the lectin with the disaccharide has been determined at 2.5 A resolution. Comparison of the structure with that of the corresponding complex with lactose reveals that the specificity of the lectin for T-antigen is generated primarily by two specific water mediated interactions, probably the first instance where water-bridges have been demonstrated to be responsi ble for generating specificity in protein-carbohydrate interactions. The elucidation of the structure of peanut lectin- T -antigen complex also provides a framework for exploring peanut lectin-based prognosis and diag nosis of certain types of carcinoma.
Item Type: | Article |
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Source: | Copyright of this article belongs to Current Science Association. |
ID Code: | 53930 |
Deposited On: | 10 Aug 2011 09:29 |
Last Modified: | 18 May 2016 06:51 |
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