Structural Analysis

MODPROPEP

MODPROPEP is a structure based program for analysis and prediction of substrates for protein kinases and MHC proteins

Improved catalytic properties of a serine hydroxymethyl transferase from Idiomarina loihiensis by site directed mutagenesis

A novel glyA gene was screened from a marine bacterium, Idiomarina loihiensis encoding a thermo-stable serine hydroxymethyl transferase (SHMT; 418 AA; 45.4 kDa). The activities of wild type (WT) and mutants were analyzed against d-phenylserine using …

Getting Phosphorylated: Is it Necessary to be Solvent Accessible?

The solvent accessibility of the Ser/Thr/Tyr containing peptide stretches in the substrate proteins of various kinases are likely to play a major role in substrate recognition by various kinases. Even though some of the computational tools make use …

Novel insights into the regulation of malarial calcium-dependent protein kinase 1

Calcium-dependent protein kinases (CDPKs) are major effectors of calcium signaling in apicomplexan parasites like Toxoplasma and Plasmodium and control important processes of the parasite life cycle. Despite recently reported crystal structures of …

Identification of substrates for Ser/Thr kinases using residue-based statistical pair potentials

**Motivation**: In silico methods are being widely used for identifying substrates for various kinases and deciphering cell signaling networks. However, most of the available phosphorylation site prediction methods use motifs or profiles derived from …

MODPROPEP: a program for knowledge-based modeling of protein–peptide complexes

MODPROPEP is a web server for knowledge-based modeling of protein–peptide complexes, specifically peptides in complex with major histocompatibility complex (MHC) proteins and kinases. The available crystal structures of protein–peptide complexes in …