| Autor: |
Alligood KJ; Glaxo Wellcome, Inc., Research Triangle Park, North Carolina 27709, USA., Charifson PS, Crosby R, Consler TG, Feldman PL, Gampe RT Jr, Gilmer TM, Jordan SR, Milstead MW, Mohr C, Peel MR, Rocque W, Rodriguez M, Rusnak DW, Shewchuk LM, Sternbach DD |
| Jazyk: |
angličtina |
| Zdroj: |
Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 1998 May 19; Vol. 8 (10), pp. 1189-94. |
| DOI: |
10.1016/s0960-894x(98)00195-4 |
| Abstrakt: |
The X-ray crystal structure of the src SH2 domain revealed the presence of a thiol residue (Cys 188) located proximal to the phosphotyrosine portion of a dipeptide ligand. An aldehyde bearing ligand (1) was designed to position an electrophilic carbonyl group in the vicinity of the thiol. X-ray crystallographic and NMR examination of the complex formed between (1) and the src SH2 domain revealed a hemithioacetal formed by addition of the thiol to the aldehyde group with an additional stabilizing hydrogen bond between the acetal hydroxyl and a backbone carbonyl. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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