STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
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STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE Descriptor: THYMIDINE PHOSPHORYLASE Authors: Pugmire, M.J, Cook, W.J, Jasanoff, A, Walter, M.R, Ealick, S.E. Deposit date: 1997-11-09 Release date: 1998-12-09 Last modified: 2024-02-14 Method: X-RAY DIFFRACTION (2.8 Å) Cite: Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J.Mol.Biol., 281, 1998
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1997-11-09



