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Crystal structure analysis of NP24-I: a thaumatin-like protein
NP24 has been reported to be anallergenic protein and an allergenic motif could be identified on the surface of the helical domain II of NP24-I, a feature common to other antifungal TLPs. Expand
Refined crystal structure (2.3 Å) of a double‐headed winged bean α‐chymotrypsin inhibitor and location of its second reactive site
The crystal structure of a double‐headed α‐chymotrypsin inhibitor, WCI, from winged bean seeds has now been refined at 2.3 Å resolution to an R‐factor of 18.7% for 9,897 reflections, leading to an understanding of the mechanism of inhibition of the protein against α‐ chymotypsin. Expand
Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K structure of winged bean chymotrypsin inhibitor (WCI) at 2.13 A resolution.
The crystal structure of a Kunitz-type double-headed alpha--chymotrypsin inhibitor from winged bean seeds has been refined at 2.13 A resolution using data collected from cryo-cooled (90 K) crystalsExpand
Structure of a Kunitz-type chymotrypsin from winged bean seeds at 2.95 A resolution.
The crystal structure of an alpha-chymotrypsin inhibitor isolated from winged bean seeds has been determined at 2.95 A resolution by the molecular-replacement method and structure refinement with RESTRAIN and X-PLOR has led to a crystallographic R factor of 19.1%. Expand
The role of Asn14 in the stability and conformation of the reactive-site loop of winged bean chymotrypsin inhibitor: crystal structures of two point mutants Asn14-->Lys and Asn14-->Asp.
Analysis of a double-headed chymotrypsin inhibitor cloned from winged bean seeds reveals that, as the Lys14 side chain takes an unusual fold in N14K and the Asp 14 side chain in N 14D interacts with the loop residues by water-mediated hydrogen bonds, the canonical conformation of the loop has remained effectively intact in both the mutant structures. Expand
Production and recovery of recombinant propapain with high yield.
This is a simple and efficient expression and purification procedure to obtain a yield of active papain, which is the highest reported so far for any recombinant plant cysteine protease. Expand
Refined Crystal Structure (2.3A°) of a Double-HeadedWinged Bean a-Chymotrypsin Inhibitor and Locationof Its Second Reactive Site
The crystal structure of a doubleheaded a-chymotrypsin inhibitor, WCI, from winged bean seeds has now been refined at 2.3A° resolution to an R-factor of 18.7% for 9,897 reflections. The crystalsExpand
Schizonts, merozoites, and phagocytosis in falciparum malaria.
This is the first documented case in which phagocytosis of malarial parasites by polymorphonuclear leukocytes is observed, and the prognostic significance of this unusual observation and the host factors that affect the survival of the patients are discussed. Expand
Structural basis of the unusual stability and substrate specificity of ervatamin C, a plant cysteine protease from Ervatamia coronaria.
In this enzyme, the nature of the S2 subsite is similar to that of papain, but at the S3 subsite, Ala67 replaces an aromatic residue, and has the effect of eliminating sufficient hydrophobic interactions required for S3-P3 stabilization, which provides the possible explanation for the lower activity of ervatamin C toward the small substrate/inhibitor. Expand