Pentamer–8I21 Fab and Pentamer–9I6 Fab interactions and structural superpositions. Pentamer–8I21 Fab and Pentamer–9I6 Fab interactions and structural superpositions.

Slides:



Advertisements
Similar presentations
Structure of an LDLR-RAP Complex Reveals a General Mode for Ligand Recognition by Lipoprotein Receptors  Carl Fisher, Natalia Beglova, Stephen C. Blacklow 
Advertisements

CsEN components reveal precisely timed cellular programs that characterize the dynamic changes of the peripheral immune system over the course of pregnancy.
Fibroblast activation in WT and NFATc2-deficient mice.
Binding of Pentamer to cells.
Comparison of ternary TCR-lipid-CD1 complex structures.
Force limits and layout design.
Self-folding triangular devices at two scales.
Comparison of predicted and measured forces and moments.
TPAD controller performance for three force components.
Cable-driven system diagram for structure matrix.
The functional and structural basis of phospholipid recognition by the PG90 TCR. The functional and structural basis of phospholipid recognition by the.
Three different types of transfer functions with a codomain of [0,1].
TPAD training protocol.
Tfr cells’ transcriptomic profile distinguishes them from Treg and Tfh cells. Tfr cells’ transcriptomic profile distinguishes them from Treg and Tfh cells.
Examples of AEGIS autonomous target selection.
Crystal structure of HCMV Pentamer.
Protein sequence alignment of the NS3 helicase–encoding region of 63 flaviviruses demonstrates conservation of a KIR2DS2-binding peptide. Protein sequence.
Analysis of Pentamer interfaces.
Visual explanation of the interaction terms.
Docking footprint of PG90 TCR on CD1b-PG.
Results of the performance study experiment: Compression (sample size: n = 5). Results of the performance study experiment: Compression (sample size: n.
Visual explanation of the interaction terms.
Structure of STAT6CF and N4 site DNA complex.
Comparison of repertoire distributions to baseline.
Fig. 1 Movement percepts for all participants.
Protein sequence alignment of the NS3 helicase–encoding region of 63 flaviviruses demonstrates conservation of a KIR2DS2-binding peptide. Protein sequence.
Comparison of ternary TCR-lipid-CD1 complex structures.
NCMs regulate T cell survival in TLOs via PD-L1.
Crystal structures of RSV G-antibody complexes.
Force limits and layout design.
Effect of slenderness on optimal shapes.
Fig. 3 Electron PSD in various regions.
Details of an implementation of a mechanism within the control chambers for selective lengthening of the sides of the soft robot. Details of an implementation.
Sequence conservation within antigenic sites γ1 and γ2, atomic interactions within the RSV G CCD, and model of RSV G glycoprotein. Sequence conservation.
Fig. 6 Comparison of properties of water models.
LC8 is structurally variable but conserved in sequence.
Fig. 2 Reference-fixing experiment, results.
Fig. 4 Structural details of tRNA binding to Elp123.
Results of the performance study experiment: Bending (sample size: n = 5). Results of the performance study experiment: Bending (sample size: n = 5). (A)
Fig. 3 Rotation experiment, setup.
Fig. 1 Cryo-EM structure of yeast Elp123 showing its active site.
Crystal structure of DS-A. 02:01 ESO 9V and WT-A
Fig. 1 Bioinspired design of AAD for promoting wound contraction.
CsEN components reveal precisely timed cellular programs that characterize the dynamic changes of the peripheral immune system over the course of pregnancy.
Comparison of predicted and measured forces and moments.
Fig. 3 Forward model. Forward model. Summary of the resampled Monte Carlo simulations shown as histograms for epoch 1 (red), epoch 2 (green), and epoch.
Fig. 4 EUV TG signal from Si.
Fig. 1 Data collection at a 40° tilt angle enabled reconstruction of a cryo-EM map of the NRTN-GFRα2-RET complex at a 5.7-Å resolution. Data collection.
AEGIS autonomous targeting process.
Examples of AEGIS autonomous target selection.
Fig. 3 ET dynamics on the control and treatment watersheds during the pretreatment and treatment periods. ET dynamics on the control and treatment watersheds.
Human Tfr cells do not express CD25.
Fig. 1 Structure of the α-SNAP–SNARE subcomplex.
by Olga Rechkoblit, Yogesh K. Gupta, Radhika Malik, Kanagalaghatta R
Fig. 4 Relationships between light and economic parameters.
Overall structure of AxqNOR and interhelical dimer interactions
Fig. 4 CO2 emission changes triggered by the JJJ clean air policy.
Fibroblast activation in WT and NFATc2-deficient mice.
Fig. 2 Large-scale μXRF and EDS characterization of the text-containing side of the TS. Large-scale μXRF and EDS characterization of the text-containing.
Fig. 3 Effects of plant species identity, plant traits, and soil properties on plant-soil feedbacks. Effects of plant species identity, plant traits, and.
Fig. 5 Superpositions of OAM.
The combined signal spectra of PSD for protons and helium nuclei
Fig. 2 Spatial distribution of five city groups.
Fig. 2 Daily TNC pickups and drop-offs for an average Wednesday in fall 2016 (1). Daily TNC pickups and drop-offs for an average Wednesday in fall 2016.
Fig. 4 The oxidized and reduced forms of the A2 domain have different dynamics and stresses. The oxidized and reduced forms of the A2 domain have different.
Fig. 4 MxB intermolecular assembly interfaces and their role in the MxB assembly and HIV-1 inhibition. MxB intermolecular assembly interfaces and their.
Fig. 6 Schematic illustration of the decreased conformational stability in the N92I mutant and its activation mechanism. Schematic illustration of the.
Fig. 1 Crystal structure of the MMOH-MMOD complex.
Fig. 4 Orthosteric ligand-binding pocket in CysLT1R.
Comparison of children’s behavior between the three conditions.
Presentation transcript:

Pentamer–8I21 Fab and Pentamer–9I6 Fab interactions and structural superpositions. Pentamer–8I21 Fab and Pentamer–9I6 Fab interactions and structural superpositions. (A) Structure of the Pentamer–8I21 Fab complex, with 8I21 HC (H) and LC (L) colored in red and teal, respectively. The boxed region on the complex is shown on the right as an “open-book” view, revealing details of the Pentamer–8I21 Fab interface. Oligomannose residues linked to Asn85 and Asn118 of UL130 are shown as sticks. (B) Details of Pentamer–8I21 Fab interactions. Residues involved in direct H-bond interactions are shown with sticks, and direct bonds are depicted with blue dashes. (C) Structure of the Pentamer–9I6 Fab complex, with Pentamer depicted as cartoon and colored as in Fig. 1 and (A), and 9I6 HC and LC depicted as brown and light blue surfaces, respectively. A top view of the 9I6 epitope on Pentamer (boxed region) is shown as surface on the right and colored according to subunits (UL128, magenta; UL131A, blue), with residues contacting the HC and LC of 9I6 colored in brown and light blue, respectively. (D) gH-based superposition of the 4.0 Å–resolution (violet) and 3.0 Å–resolution (cyan) Pentamer–8I21 Fab and of the 9I6 (gold) and the 3.0 Å–resolution 8I21 (cyan) complexes viewed from the side and from the top. A UL130/ UL131A-based superposition of the 9I6 (gold) and the 3.0 Å–resolution 8I21 (cyan) Fab complexes is also shown in the upper right panel. Blue semitransparent arrows in (D) show the movements of secondary structure elements. Sumana Chandramouli et al. Sci. Immunol. 2017;2:eaan1457 Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.