The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of antibodies and T cell receptors
- D. Y. Lin, Yoshimasa Tanaka, D. Garboczi
- BiologyProceedings of the National Academy of Sciences
- 26 February 2008
The PD-1/PD-L1 interaction described here may be blocked by antibodies or by designed small-molecule drugs to lower inhibitory signaling that results in a stronger immune response.
Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer
- M. Adachi, J. Kanamori, S. Utsumi
- ChemistryProceedings of the National Academy of Sciences…
- 27 May 2003
Electrostatic analysis of the faces suggests that the interchain disulfide-containing face has high positive potential at acidic pH, which induces dissociation of the hexamer into trimers that may be susceptible to proteinases after seed imbibition.
Crystal structure of soybean proglycinin A1aB1b homotrimer.
- M. Adachi, Y. Takenaka, A. Gidamis, B. Mikami, S. Utsumi
- ChemistryJournal of Molecular Biology
- 12 January 2001
The crystal structure of proglycinin is similar to those of canavalin and phaseolin belonging to the 7 S globulin family, strongly supporting the hypothesis that both 7 S and 11 S globulins are derived from a common ancestor.
Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release.
It is proposed that uptake of the Fe(3+)-transferrin complex into an acidic endosome via receptor-mediated endocytosis will result in the protonation of both lysine residues, which lies below the pH of the structure determination and is, therefore, not positively charged.
A structural basis for depolymerization of alginate by polysaccharide lyase family-7.
A Redox-controlled Molecular Switch Revealed by the Crystal Structure of a Bacterial Heme PAS Sensor*
A novel redox-regulated molecular switch is proposed in which local heme-ligand switching may trigger a global “scissor-type” subunit movement that facilitates catalytic control of Escherichia coli redox sensor.
Crystal Structure of Exotype Alginate Lyase Atu3025 from Agrobacterium tumefaciens*
- A. Ochiai, M. Yamasaki, B. Mikami, W. Hashimoto, K. Murata
- Chemistry, BiologyJournal of Biological Chemistry
- 27 May 2010
The structural analysis of H531A/ΔGGG and subsequent site-directed mutagenesis studies proposed the enzyme reaction mechanism, with His311 and Tyr365 as the catalytic base and acid, respectively.
Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III.
- B. Mikami, M. Ban, K. Murata
- Chemistry, BiologyActa Crystallographica Section D: Biological…
- 1 September 2012
The structures of two mutants of a mannuronate-specific alginate lyase, A1-III, from Sphingomonas species A1 complexed with a tetrasaccharide substrate were determined by X-ray crystallography at around 2.2 Å resolution together with the apo form of the H192A mutant.
Crystal Structure of Plant Ferritin Reveals a Novel Metal Binding Site That Functions as a Transit Site for Metal Transfer in Ferritin*
A comparison of the ferroxidase activities of the native and the E173A mutant of SFER4 clearly showed a delay in the iron oxidation rate of the mutant, which indicated that the glutamate residue functions as a transit site of iron from the 3-fold entry channel to the feroxidase site, which may be universal among ferritins.