Protein Science

Cover image for Vol. 26 Issue 2

Edited By: Brian W. Matthews

Impact Factor: 3.039

ISI Journal Citation Reports © Ranking: 2015: 118/289 (Biochemistry & Molecular Biology)

Online ISSN: 1469-896X

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  • Oligomerization domains in the glycan-binding receptors DC-SIGN and DC-SIGNR: Sequence variation and stability differences

    Oligomerization domains in the glycan‐binding receptors DC‐SIGN and DC‐SIGNR: Sequence variation and stability differences

    Comparison of the sequences of neck domains from DC-SIGN homologs in various primates. Residues at positions 6 and 15 of the repeat units are indicated in single-letter amino acid code, with those that stabilize the tetrameric coiled-coil, leucine at position 6 and arginine at position 15, highlighted in yellow. Repeat units that contain leucine at position 6 are colored green, repeat units that contain glutamine at this position are colored pink and repeat units that contain methionine are colored cyan. The unusual repeat units at the C-terminus of the neck domain of DC-SIGNR are colored orange. Non-repeat regions at the N-terminus are indicated by purple rectangles. (A) DC-SIGN neck domain organization. (B) DC-SIGNR neck domain organization.

  • Mercury(II) binds to both of chymotrypsin's histidines, causing inhibition followed by irreversible denaturation/aggregation

    Mercury(II) binds to both of chymotrypsin's histidines, causing inhibition followed by irreversible denaturation/aggregation

    Structure of α-chymotrypsin (PDB# 4Q2K): (A) front view; (B) rear view.

  • Human CaaX protease ZMPSTE24 expressed in yeast: Structure and inhibition by HIV protease inhibitors

    Human CaaX protease ZMPSTE24 expressed in yeast: Structure and inhibition by HIV protease inhibitors

    Lipid-like densities. Electron density and modeled detergent and phospholipid molecules are represented by the mesh and the molecular stick representations. The figure was generated as a 2Fo-Fc map using mesh at a contour level of 1.0σ showing all electron density within a distance of 2.0 Å of the modeled lipids and detergents.

  • The IDL of E. coli SSB links ssDNA and protein binding by mediating protein–protein interactions

    The IDL of E. coli SSB links ssDNA and protein binding by mediating protein–protein interactions

    SSB linkers mediate all protein–protein interactions. Schematics of wild type SSB proteins binding to ssDNA and to partners. The colouring of SSB monomers is as follows the core domain in green, linker in blue and acidic tip in red. Here tetramers have their functional C-terminal domains exposed in solution. Upon binding to ssDNA the IDLs of monomers 1 and 2, bind to the OB-folds of monomers 1′ and 2′, respectively. Concurrently, the linkers of monomers 1′ and 2′ bind to the OB-folds of monomers 3 and 4, and their IDLs bind to monomers 3′and 4′, respectively. The C-termini of subunits 3′ and 4′ are available to bind to an incoming tetramer as shown on the right. On the opposite side of each tetramer, C-termini are available for binding to interactome partners such as RecG or RecO (purple and blue ovals). For simplicity, SSB–SSB interactions are shown in the top subunits only, and SSB interactome partners binding in the lower subunits.

  • Effect of fuel concentration and force on collective transport by a team of dynein motors

    Effect of fuel concentration and force on collective transport by a team of dynein motors

    (A) Schematic diagram of cargo transport by a team of dynein motors along -end of a microtubule with N = 4. (B) Schematic of the various ATP binding sites of the single dynein motor head. ATP can bind to site 1, 2, 3, and 4 however it can get hydrolyzed only at site 1.

  • Phosphorylation of KLHL3 at serine 433 impairs its interaction with the acidic motif of WNK4: a molecular dynamics study

    Phosphorylation of KLHL3 at serine 433 impairs its interaction with the acidic motif of WNK4: a molecular dynamics study

    The initial positions of modeled phosphorylated S433 (pS433) in the Kelch domain of KLHL3 (residues 300–585, in yellow) and residues in the acidic motif (AM, residues 557 − 565, in purple) of WNK4. In the top view (upper right), the six Kelch repeats in the Kelch domain of KLHL3 are labeled as I–VI, and four antiparallel β-strands in repeat I are labeled as 1–4. The black dashed rectangle represents the AM-binding site on Kelch domain of KLHL3, and the green dot circle represents the location of pS433 in the top view. For clarity, residues of the AM in WNK4 and pS433 of KLHL3 are enlarged (lower right). The pS433 residue is located in the pocket formed by the side chain of P561, main chain of E562 and both main and side chains of A563 in the AM of WNK4. For simplicity, the hydrogen atoms in the side chain of AM are not shown.

  • Oligomerization domains in the glycan‐binding receptors DC‐SIGN and DC‐SIGNR: Sequence variation and stability differences
  • Mercury(II) binds to both of chymotrypsin's histidines, causing inhibition followed by irreversible denaturation/aggregation
  • Human CaaX protease ZMPSTE24 expressed in yeast: Structure and inhibition by HIV protease inhibitors
  • The IDL of E. coli SSB links ssDNA and protein binding by mediating protein–protein interactions
  • Effect of fuel concentration and force on collective transport by a team of dynein motors
  • Phosphorylation of KLHL3 at serine 433 impairs its interaction with the acidic motif of WNK4: a molecular dynamics study

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Author Shigeki Arai on his recently published Protein Science paper entitled " An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody." Read the paper here

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2016 Best Paper Award Winners
We are pleased to announce the winners of the 2016 Protein Science Best Paper Award:

Tracy Clinton
Air Force Biochemist

Design and characterization of ebolavirus GP prehairpin intermediate mimics as drug targets
Tracy R. Clinton, Matthew T. Weinstock, Michael T. Jacobsen, Nicolas Szabo-Fresnais, Maya J. Pandya, Frank G. Whitby, Andrew S. Herbert, Laura I. Prugar, Rena McKinnon, Christopher P. Hill, Brett D. Welch, John M. Dye, Debra M. Eckert and Michael S. Kay
Protein Sci. 24:446-463, 2015.

Michael Thompson
Postdoctoral Fellow
Department of Bioengineering and Therapeutic Sciences at University of California, San Francisco

An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein
Michael C. Thompson, Duilio Cascio, David J. Leibly and Todd O. Yeates
Protein Sci. 24:956-975, 2015.

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2016 Young Investigator Award Winner

The Protein Science Young Investigator Award recognizes a scientist generally within the first 8 years of an independent career who has made an important contribution to the study of proteins. The 2016 winner is Dr. Benjamin Garcia (University of Pennsylvania Perelman School of Medicine).

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More information on our awards can be found here.

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