Zhiwei Chen
Saint Louis University
26 Papers
214 Citations
Zhiwei Chen is an academic researcher from Saint Louis University. The author has contributed to research in topics: Thrombin & Active site. The author has an hindex of 16, co-authored 26 publications.
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Papers
Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation
TL;DR: A theoretical analysis and an improved refinement of the 1.9-A resolution crystal structure of MDH from Methylophilus methylotrophus W3A1 in the presence of methanol indicates that the observed tetrahedral configuration of the C-5 atom of PQQ in that study represents theC-5-reduced form of the cofactor and lends support for a hydride transfer mechanism for MDH.
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Crystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4.
TL;DR: The structures demonstrate that thrombin activation of PAR4 may occur with exosite I available to bind cofactor molecules, like the cleaved form of PAR3, whose function is to promote substrate diffusion into the active site by allosterically changing the conformation of the 60-loop.
Crystal structure of thrombin bound to the uncleaved extracellular fragment of PAR1.
TL;DR: The structure of thrombin S195A in complex with a 30-residue long uncleaved extracellular fragment of PAR1 is presented that documents for the first time a productive binding mode bridging the active site and exosite I and reveals two unexpected features of the throm bin-PAR1 interaction.
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Crystallographic and Kinetic Evidence of Allostery in a Trypsin-like Protease.
Weiling Niu,Zhiwei Chen,Prafull S. Gandhi,Austin D. Vogt,Nicola Pozzi,Leslie A. Pelc,Fatima Zapata,Enrico Di Cera +7 more
TL;DR: In this paper, a structural validation of a pre-existing equilibrium between alternative conformations remains a challenge even for textbook examples of allosteric proteins (e.g., trypsin-like proteins).
Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation.
TL;DR: The first x-ray crystal structure of prothrombin as a Gla-domainless construct carrying an Ala replacement of the catalytic Ser-525 is reported, indicating a structure-based mechanism of prohrombin activation emerges.
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