U.S. Department of Health and Human Services
Jenny Hinshaw
 

 Contact Info

 
Tel: 301-594-0842
Email: jennyh@helix.nih.gov
 

 Select Experience

 
  • Ph.D.Brown University1989
  • B.A.Wellesley College1982
 

 Related Links

 
Specialties
  • Cell Biology/Cell Signaling
  • Structural Biology

​Research Images

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TitleDescriptionImage
Reconstruction of DeltaPRD dynamin in the constricted state reveals new structural features of the assembled dynamin polymerTwo density thresholds of the DeltaPRD map are shown: the lower threshold is colored gray, and the higher threshold is in mesh and colored radially to denote the locations of the PH domain (yellow), Middle/GED (blue), and GTPase (green) regions. The top left panel shows a cross-section through PRD polymer; it depicts the classical ‘‘T view’’ of dynamin subunits within individual helical rungs. The top right panel shows a surface view of the GTPase domains (green, labeled Head) and an inner view of the Middle/GED region (blue). The bottom left panel is an end-on view of the tube looking down the helical axis, and the bottom right panel is a side view of the helical assembly. (see Chappie et al., 2012)Reconstruction of DeltaPRD dynamin in the constricted state reveals new structural features of the assembled dynamin polymerEnlarge
Docked dynamin tetramers reveal mechanism of constrictionThis image depicts the assembly of long dynamin tetramer models within the GMPPCP-stabilized constricted PRD map (gray). The numbering and rainbow coloring (red to blue) denote the sequential addition of tetramers, and terminates when the first G domain dimer is formed. The left panel depicts a top view of the long assembly looking down the helical axis; the right panel is a side view perpendicular to this axis. The sequential rungs of the dynamin helix are marked in the lower panel with black brackets and numbered as ‘‘1’’ and ‘‘2.’’ The dashed black box highlights the partnering helical rungs facilitating G domain dimerization. (see Chappie et al., 2012)Docked dynamin tetramers reveal mechanism of constrictionEnlarge
Dnm1 constricts the underlying lipid bilayer upon addition of GTPAs shown on the left, the Dnm1 assembles onto liposomes to form large protein-lipid tubes with a diameter of ~130 nm. Upon GTP addition, the tubes constrict to ~60 nm, as shown in the right panel. Dnm1 constricts the underlying lipid bilayer upon addition of GTPEnlarge