| Autor: |
Zhang, Zhen, Qian, Minxie, Huang, Qichen, Jia, Yisi, Tang, Youqi, Wang, Keyi, Cui, Dafu, Li, Moyi |
| Zdroj: |
Journal of Protein Chemistry; Jan2001, Vol. 20 Issue 1, p59-65, 7p |
| Abstrakt: |
The X-ray structure analysis of a cross-linked crystal of concanavalin A soaked with the tripeptide molecule as the probe molecule showed electron density corresponding to full occupation in the binding pocket. The site lies on the surface of concanavalin A and is surrounded by three symmetry-related molecules. The crystal structure of the tripeptide complex was refined at 2.4-Å resolution to an R-factor of 17.5%, (Rfree factor of 23.7%), with an RMS deviation in bond distances of 0.01 Å. The model includes all 237 residue of concanavalin A, 1 manganese ion, 1 calcium ion, 161 water molecules, 1 glutaraldehyde molecule, and 1 tripeptide molecule. This X-ray structure analysis also provides an approach to mapping the binding surface of crystalline protein with a probe molecule that is dissolved in a mixture of organic solvent with water or in neat organic solvent but is hardly dissolved in aqueous solution. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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