Research Topics
| Weikai LiSummaryAffiliation: Harvard University Country: USA Publications
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Detail Information
Publications
Structure of a bacterial homologue of vitamin K epoxide reductaseWeikai Li
Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Nature 463:507-12. 2010..Our results have implications for the mechanism of the mammalian VKOR and explain how mutations can cause resistance to the VKOR inhibitor warfarin, the most commonly used oral anticoagulant...
The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane sealWeikai Li
Howard Hughes Medical Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA
Mol Cell 26:511-21. 2007..Our data show that the plug domain is required to maintain a closed state of the channel and suggest a mechanism for channel gating...
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partnersSol Schulman
Department of Cell Biology, Harvard Medical School, Howard Hughes Medical Institute, 240 Longwood Avenue, Boston, MA 02115, USA
Proc Natl Acad Sci U S A 107:15027-32. 2010..Taken together, our results demonstrate that human VKOR employs the same electron transfer pathway as its bacterial homologs and that VKORs generally prefer membrane-bound Trx-like redox partners...
Crystal structure of an unusual thioredoxin protein with a zinc finger domainJiqing Ye
Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
J Biol Chem 282:34945-51. 2007..On the basis of structural similarity to the zinc fingers in Npl4 and Vps36, we propose that the N-terminal zinc finger of thioredoxin-2 mediates protein-protein interactions, possibly with its substrates or chaperones...
A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecAJochen Zimmer
Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA
J Mol Biol 364:259-65. 2006..subtilis SecA suggests that small changes in the nucleotide binding domains could be amplified via helix 1 of the helical scaffold domain (hsd) to generate larger movements of the domains involved in polypeptide binding...
