Inhibitor of parasitic TS-DHFR enzyme discovered by virtual library screening.
Image from the Anderson lab.
A view of the Oceanobacillus iheyensis group II intron. This is a large ribozyme RNA that catalyzes its own self-splicing and retrotransposition. It has an elaborate tertiary architecture that reveals new principles for RNA folding and structural packing.
Image from the Pyle lab.
Structure of the cerebral cavernous malformation-associated protein, CCM3 (PDCD10), showing a novel dimerization fold.
Image from the Boggon lab.
Artistic rendering of dengue virus immediately prior to the fusion of the viral lipid membrane (bottom) to the endosomal membrane of the host cell (top). Two dengue virus envelope protein trimers are shown (in surface representation) on either side of a nascent membrane fusion stalk. Completion of membrane fusion requires the alpha-helical “stem” regions (shown in worm representation) to anneal onto the core of the E trimers. The image is based on crystal structures of dengue virus E protein in the postfusion conformation determined in the Modis Laboratory. Image created by Janet Iwasa and Gaël McGill, Digizyme, Inc.
Vinod Nayak, Moshe Dessau, Kaury Kucera, Karen Anthony, Michel Ledizet & Yorgo Modis (2009). Crystal structure of dengue type 1 envelope protein in the postfusion conformation and its implication for receptor binding, membrane fusion and antibody recognition. J. Virol., 83, 4338-44.
Yorgo Modis, Steven Ogata, David Clements & Stephen C. Harrison (2004). Structure of the dengue virus envelope protein after membrane fusion. Nature, 427, 313-319.
Image from the Modis lab.
Three-dimensional reconstruction of the yeast Rrp44-exosome complex with atomic models docked in the map.
Image from the Wang lab.
From cryo-EM images of channel proteins in liposomes, a 3D reconstruction of the BK potassium channel. On the left is a cryo-EM image of liposomes 250 and 400 A in diameter. On the right, the BK map (gray mesh) with densities from X-ray structures of the Kv1.2 potassium channel and the MthK gating ring docked. The light mesh shows the membrane density. From L. Wang & F. J. Sigworth, Nature 2009.
Image from the Sigworth lab.
Shown here are the six transmembrane helices of GlpG, the first intramembrane protease with its crystal structure determined.
Image from the Ha lab.
Electron density for the Oceanobacillus iheyensis group II intron structure, with a trace shown for the RNA backbone. This is a large ribozyme RNA that catalyzes its own self-splicing and retrotransposition. It has an elaborate tertiary architecture that reveals new principles for RNA folding and structural packing.
A cutaway view of the large ribosomal subunit with three tRNA molecules showing many antibiotics bound in the exit tunnel near the peptidyl transferase center. The A-site, P-site and E-site tRNAs are colored in red, orange and yellow, respectively. The rRNA is in white, protein penetrating the RNA is shown in yellow and a model of a polypeptide exiting down the tunnel is shown. A macrolide bound in the tunnel in a position to block the exiting peptide is shown in dark blue.
Image from the Steitz lab.
Structure of PINCH1 LIM1 domain in complex with Integrin-linked kinase ankyrin repeat domain.
X-ray crystallographic structure of the extracellular domain of the human prolactin receptor bound to the high-affinity binding-site of a prolactin variant. Four histidine residues responsible for pH-dependent regulation of receptor recognition are shown.
Image from the Hodsdon lab.
The invariant guanosine within the group II intron active-site is engaged on both the major groove and minor groove edges in a network of critical hydrogen bonds.
Crystal structure of LeuT, a bacterial homologue of the serotonin transporter, complexed with its substrates (leucine and 2 sodium ions) and an inhibitor (the tricyclic antidepressant clomipramine). Leucine is yellow, red, and blue; sodium ions are cyan; and clomipramine is yellow and green.
Image from the Singh lab.
Sulfate binding in the tunnel of MIF.
Image from the Lolis lab.
The amyloid plaque indicator fluor, thioflavin T (shown in orange), intercalated between beta sheets of the protein, beta-2-microglobulin.
Image from the Miranker lab.
Atomic model of West Nile virus based on the crystal structure of the major envelope glycoprotein E determined in the Modis Laboratory. The packing of E molecules on the viral surface is derived from an electron cryomicroscopy image reconstruction of dengue type 2 virus.
Ryuta Kanai, Kalipada Kar, Karen Anthony, L. Hannah Gould, Michel Ledizet, Erol Fikrig, Wayne A. Marasco, Ray A. Koski & Yorgo Modis (2006). Crystal structure of West Nile virus envelope glycoprotein reveals viral surface epitopes. J. Virol., 80, 11000-8.
Wei Zhang, Paul R Chipman, Jeroen Corver, Peter R Johnson, Ying Zhang, Suchetana Mukhopadhyay, Timothy S Baker, James H Strauss, Michael G Rossmann & Richard J Kuhn (2003). Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nat. Struct. Biol., 10, 907-12.
Close up of a designed TPR-peptide interaction interface.
Image from the Regan lab.
Extracellular domain structures of Receptor Tyrosine Kinases. (Front) The ternary complex structure of Fibroblast Growth Factor Receptor 1 (FGFR1) extracellular domain in complex with FGF2 and heparin. Two FGF2 molecules are colored in green, and two D2-D3 domains of FGFR1 in magenta and yellow. The heparin molecules are depicted in stick. (Back) The extracellular domain structure of KIT dimer in complex with Stem Cell Factor dimer (SCF). SCF dimer mediates the complex formation of KIT extracellular domains. Five Ig-like domains of KIT extracellular domains are colored in blue, green, yellow, orange, and pale pink from D1 to D5, respectively. SCF dimer is colored in magenta.
Image from the Schlessinger lab.
Activated Fibroblast Growth Factor Receptor 1 (FGFR1) in complex with tandem SH2 domains of Phospholipase Cγ (PLCγ). From far to near, the picture shows progression of the complex formation between FGFR1 and PLCγ. The kinase domain of FGFR1 in colored in green, N-terminal SH2 domain of PLCγ in cyan, and C-terminal SH2 domain in dark blue. An ATP and the substrate peptide are shown in stick, and a magnesium ion (Mg) in blue sphere. The canonical phosphorylation-dependant primary binding site colored in blue is found between FGFR1 and PLCγ. In addition, the novel phosphorylation-independent secondary binding site colored in red is found in the complex structure.
The guanine nucleotide exchange factor Sec2p (purple) activating the Rab GTPase (white). See Dong et al (2007) in Molecular Cell 25: 455-62.
Image from the Reinisch lab.
The activity of the pro-inflammatory protein macrophage migration inhibitory factor (MIF) is modulated by the non-competitive inhibitor ibudilast and its derivative AV1013. These compounds bind in an allosteric cleft not seen in the unbound MIF structure. The allosteric site is proximal to the active site, explaining the mode of inhibition. Image courtesy of Yoonsang Cho.
Binding pocket of the c-di-GMP riboswitch.
Image from the Strobel lab.
The NPP (nucleotide pyrophosphatase/phosphodiesterase) family of proteins is involved in a large variety of functions, including angiogenesis, bone mineralization and the metastasis of various cancers. The Braddock lab is utilizing X-ray crystallography in the pursuit of structure/function studies on some of the these family members. The image shows an NPP family member with a product molecule (red) bound in the active site.
Image from the Braddock lab.
Model of a potential viral tethering mode by human antiviral protein thetherin.
Image from the Xiong lab.
NMR solution structure of a thiopurine methyltransferase (TPMT) bacterial orthologue, colored according to the degree of dynamic conformational changes associated with binding S-adenosylmethionine. In humans, TPMT metabolizes 6-thiopurine medications and single-site amino acid polymorphisms in the enzyme are associated with variations in both drug efficacy and toxicity.
The guanine nucleotide exchange factor (GEF) core of the TRAPPI membrane tethering complex activating the Rab GTPase Ypt1p (yellow). See Cai et al (2008). Cell 133: 1202-1213
This is a structural element within Domain 1 of the Oceanobacillus iheyensis group II intron. This motif represents and example of "RNA inside-out", in which the sugar-phosphate backbone of one strand is in the center, with its bases interacting side-to-side with two other strands.