Preparation of a protein-dimerizing ligand by topochemistry and structure-based design

Journal of the American Chemical Society

Volumn 118, Issue 10, 1996, Pages 2535-2536

  Katz, Bradley A ^a  

^a Arris Pharmaceutical Corporation   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PROTEIN SYNTHESIS; TECHNIQUE;

EID: 0029990033     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9536936     Document Type: Article

References (18)

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2. Giebel, L. B.; Cass, R. T.; Milligan, D.; Young, D.; Arze, R.; Johnson, C. Biochemistry 1995, 34, 15430-15435.
3. Katz, B. A. Biochemistry 1995, 34, 15421-15429.
4. Katz, B. A.; Cass, R. T.; Liu, B.; Arze, R.; Collins, N. J. Biol. Chem. 1995, 270, 31210-31218.
5. Standard deviations are derived from 7-15 independent determinations.
6. Structures were refined with Xplor (Brünger, A. T. X-PLOR Manual, version 3.0; Yale University: New Haven. CT. 1992) and with difference Fourier methods (Chambers, J. L.; Stroud, R. M. Acta Crystallogr. 1979, B33. 1861). Water structure was determined and refined according to published procedures (Finer-Moore, J. S.; Kossiakoff, A. A.; Hurley, J. H.; Earnest, T.; Stroud, R. M. Proteins 1992, 12, 203-222).
7. Structures were refined with Xplor (Brünger, A. T. X-PLOR Manual, version 3.0; Yale University: New Haven. CT. 1992) and with difference Fourier methods (Chambers, J. L.; Stroud, R. M. Acta Crystallogr. 1979, B33. 1861). Water structure was determined and refined according to published procedures (Finer-Moore, J. S.; Kossiakoff, A. A.; Hurley, J. H.; Earnest, T.; Stroud, R. M. Proteins 1992, 12, 203-222).
8. Structures were refined with Xplor (Brünger, A. T. X-PLOR Manual, version 3.0; Yale University: New Haven. CT. 1992) and with difference Fourier methods (Chambers, J. L.; Stroud, R. M. Acta Crystallogr. 1979, B33. 1861). Water structure was determined and refined according to published procedures (Finer-Moore, J. S.; Kossiakoff, A. A.; Hurley, J. H.; Earnest, T.; Stroud, R. M. Proteins 1992, 12, 203-222).
9. 2, calculated phases.
10. The average Cα-Cα distance for disulfide-bonded residues in the Brookhaven Data Base is 5.45 (0.63) Å (Katz, B. A.; Kossiakoff, A. A. J. Biol. Chem. 1986, 261, 15480-15485).
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