Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms
Author:
Affiliation:
1. Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference51 articles.
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2. BARGONETTI, J, WILD-TYPE BUT NOT MUTANT P53 IMMUNOPURIFIED PROTEINS BIND TO SEQUENCES ADJACENT TO THE SV40 ORIGIN OF REPLICATION, CELL 65: 1083 (1991).
3. BARGONETTI, J, A PROTEOLYTIC FRAGMENT FROM THE CENTRAL REGION OF P53 HAS MARKED SEQUENCE-SPECIFIC DNA-BINDING ACTIVITY WHEN GENERATED FROM WILD-TYPE BUT NOT FROM ONCOGENIC MUTANT P53-PROTEIN, GENES & DEVELOPMENT 7: 2565 (1993).
4. Crystallographic R Factor Refinement by Molecular Dynamics
5. X-PLOR v3.1 Manual 1990
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