Simon Terzyan

Summary

Affiliation: University of Oklahoma Health Sciences Center
Country: USA

Publications

  1. ncbi request reprint High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop
    Guangyu Zhu
    Crystallography Research Program of Oklahoma Medical Research Foundation, Oklahoma City 73104, USA
    J Biol Chem 278:2452-60. 2003
  2. ncbi request reprint A histidine/tryptophan pi-stacking interaction stabilizes the heme-independent folding core of microsomal apocytochrome b5 relative to that of mitochondrial apocytochrome b5
    Lijun Wang
    Department of Chemistry, University of Kansas, Lawrence, Kansas 66045, USA
    Biochemistry 45:13750-9. 2006
  3. ncbi request reprint Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution
    Simon Terzyan
    Crystallography Research Program of Oklahoma Medical Research Foundation, 825 NE 13th Street, Oklahoma City, OK 73104, USA
    Acta Crystallogr D Biol Crystallogr 60:54-60. 2004
  4. ncbi request reprint Crystal structure of the human GGA1 GAT domain
    Guangyu Zhu
    Crystallography Research Program and Protein Studies Program, Oklahoma Medical Research Foundation, 825 Northeast 13th Street, Oklahoma City, Oklahoma 73104, USA
    Biochemistry 42:6392-9. 2003
  5. ncbi request reprint Structural basis of Rab5-Rabaptin5 interaction in endocytosis
    Guangyu Zhu
    Crystallography Research Program, Oklahoma Medical Research Foundation, 825 N E 13th Street, Oklahoma City, Oklahoma 73104, USA
    Nat Struct Mol Biol 11:975-83. 2004
  6. pmc Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5
    Guangyu Zhu
    Crystallography Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA
    EMBO J 26:3484-93. 2007
  7. ncbi request reprint Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain
    Simon Terzyan
    Crystallography Research Program, Oklahoma Medical Research Foundation, 825 NE 13th Street, Oklahoma City, Oklahoma 73104, USA
    Proteins 56:277-84. 2004
  8. pmc Inhibition of anthrax lethal factor: lability of hydroxamate as a chelating group
    Feng Li
    Protein Studies Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA
    Appl Microbiol Biotechnol 94:1041-9. 2012
  9. ncbi request reprint Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket
    Guangyu Zhu
    Crystallography Research Program of Oklahoma Medical Research Foundation, 825 N E 13th Street, Oklahoma City 73104, USA
    FEBS Lett 537:171-6. 2003
  10. pmc Lethal factor of anthrax toxin binds monomeric form of protective antigen
    Irina Chvyrkova
    Crystallography Research Program, Oklahoma Medical Research Foundation, 825 N E 13th Street, Oklahoma City, OK 73104, USA
    Biochem Biophys Res Commun 360:690-5. 2007

Collaborators

Detail Information

Publications18

  1. ncbi request reprint High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop
    Guangyu Zhu
    Crystallography Research Program of Oklahoma Medical Research Foundation, Oklahoma City 73104, USA
    J Biol Chem 278:2452-60. 2003
    ....
  2. ncbi request reprint A histidine/tryptophan pi-stacking interaction stabilizes the heme-independent folding core of microsomal apocytochrome b5 relative to that of mitochondrial apocytochrome b5
    Lijun Wang
    Department of Chemistry, University of Kansas, Lawrence, Kansas 66045, USA
    Biochemistry 45:13750-9. 2006
    ..We also present evidence indicating that the conserved Mc b5 packing motif noted above contributes to the unusually extensive secondary structure exhibited by bovine Mc apo-b5 in the urea-denatured state...
  3. ncbi request reprint Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution
    Simon Terzyan
    Crystallography Research Program of Oklahoma Medical Research Foundation, 825 NE 13th Street, Oklahoma City, OK 73104, USA
    Acta Crystallogr D Biol Crystallogr 60:54-60. 2004
    ..Furthermore, residues of multiple conformation and clustered distribution of anisotropic thermal motions of the protein molecule may have general implications for the function of Ras-like GTPases...
  4. ncbi request reprint Crystal structure of the human GGA1 GAT domain
    Guangyu Zhu
    Crystallography Research Program and Protein Studies Program, Oklahoma Medical Research Foundation, 825 Northeast 13th Street, Oklahoma City, Oklahoma 73104, USA
    Biochemistry 42:6392-9. 2003
    ..These structural characteristics are consistent with a model supporting multiple functional roles for the GAT domain...
  5. ncbi request reprint Structural basis of Rab5-Rabaptin5 interaction in endocytosis
    Guangyu Zhu
    Crystallography Research Program, Oklahoma Medical Research Foundation, 825 N E 13th Street, Oklahoma City, Oklahoma 73104, USA
    Nat Struct Mol Biol 11:975-83. 2004
    ..Biochemical and functional analyses show that the crystallographically observed Rab5-Rabaptin5 complex also exists in solution, and disruption of this complex by mutation abrogates endosome fusion...
  6. pmc Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5
    Guangyu Zhu
    Crystallography Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA
    EMBO J 26:3484-93. 2007
    ..On the Rab5 side, both switch regions are involved in the interaction. Thus we identified a new binding mode between PH domains and small GTPases...
  7. ncbi request reprint Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain
    Simon Terzyan
    Crystallography Research Program, Oklahoma Medical Research Foundation, 825 NE 13th Street, Oklahoma City, Oklahoma 73104, USA
    Proteins 56:277-84. 2004
    ..Combined with other biochemical data, these results support the premise that Lys-698 of human Pg plays a functional role in the so-called N-terminal insertion activation mechanism by SK...
  8. pmc Inhibition of anthrax lethal factor: lability of hydroxamate as a chelating group
    Feng Li
    Protein Studies Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA
    Appl Microbiol Biotechnol 94:1041-9. 2012
    ..These results suggest that in the development of new LF inhibitors, the stability of the chelating group should be carefully examined and that DMHA is a potentially useful moiety to be used in new LF inhibitors...
  9. ncbi request reprint Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket
    Guangyu Zhu
    Crystallography Research Program of Oklahoma Medical Research Foundation, 825 N E 13th Street, Oklahoma City 73104, USA
    FEBS Lett 537:171-6. 2003
    ..Thus, the current structure suggests that a conformational change induced by ligand binding occurs in this part of the ligand pocket...
  10. pmc Lethal factor of anthrax toxin binds monomeric form of protective antigen
    Irina Chvyrkova
    Crystallography Research Program, Oklahoma Medical Research Foundation, 825 N E 13th Street, Oklahoma City, OK 73104, USA
    Biochem Biophys Res Commun 360:690-5. 2007
    ..In addition, we demonstrated that the PA20 directly interacts with the LF-N domain. Our data points to an alternative process of self-assembly of anthrax toxin on the surface of host cells...
  11. pmc The major neutralizing antibody responses to recombinant anthrax lethal and edema factors are directed to non-cross-reactive epitopes
    Melissa L Nguyen
    Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA
    Infect Immun 77:4714-23. 2009
    ..This work increases understanding of the immunogenicity of EF and LF and offers perspective for the development of new strategies for vaccination against anthrax...
  12. doi request reprint Using substrate specificity of antiplasmin-cleaving enzyme for fibroblast activation protein inhibitor design
    Kyung N Lee
    William K Warren Research Center and Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73126, USA
    Biochemistry 48:5149-58. 2009
    ..Results indicate that Arg at P5, P6, or P7 distances from P1 enhances affinity and efficiency of substrates or inhibitors toward APCE or FAP...
  13. pmc Subsite specificity of anthrax lethal factor and its implications for inhibitor development
    Feng Li
    Protein Studies, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA
    Biochem Biophys Res Commun 407:400-5. 2011
    ..For better use of the new findings for inhibitor design, we have modeled the most preferred residues in the active site of lethal factor. The observed interactions provide new insights to future inhibitor designs...
  14. ncbi request reprint Three-dimensional structures of idiotypically related Fabs with intermediate and high affinity for fluorescein
    Simon Terzyan
    Crystallography Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA
    J Mol Biol 339:1141-51. 2004
    ....
  15. doi request reprint Putative sequences on Ro60 three-dimensional structure accessible for 4-hydroxy-2-nonenal (HNE) modification compared to in vitro HNE modification of Ro60 sequences
    Biji T Kurien
    Arthritis and Clinical Immunology Program, Oklahoma Medical Research Foundation, Oklahoma, OK 73104, USA
    Mol Immunol 50:185-92. 2012
    ....
  16. ncbi request reprint Comparison of cytochromes b5 from insects and vertebrates
    Lijun Wang
    Department of Chemistry, University of Kansas, Lawrence, Kansas 66045, USA
    Proteins 67:293-304. 2007
    ....
  17. ncbi request reprint Toward engineering the stability and hemin-binding properties of microsomal cytochromes b5 into rat outer mitochondrial membrane cytochrome b5: examining the influence of residues 25 and 71
    Aaron B Cowley
    Department of Chemistry, University of Kansas, Lawrence, KS 66045 7582, USA
    Biochemistry 41:11566-81. 2002
    ....
  18. ncbi request reprint The crystal structure of the endothelial protein C receptor and a bound phospholipid
    Vaheh Oganesyan
    Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104, USA
    J Biol Chem 277:24851-4. 2002
    ..The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome...