Home  About us  Contact
 

EVH1 Domain (evh1 + domain)

Distribution by Scientific Domains
Chemistry100%

Selected Abstracts

Structure-Based Synthetic Mimicry of Discontinuous Protein Binding Sites: Inhibitors of the Interaction of Mena EVH1 Domain with Proline-Rich Ligands

CHEMBIOCHEM, Issue 8 2006
Cornelia Hunke Dr.
Abstract The Mena EVH1 domain, a protein-interaction module involved in actin-based cell motility, recognizes proline-rich ligand motifs, which are also present in the sequence of the surface protein ActA of Listeria monocytogenes. The interaction of ActA with host Mena EVH1 enables the bacterium to actively recruit host actin in order to spread into neighboring cells. Based on the crystal structure of Mena EVH1 in complex with a polyproline peptide ligand, we have generated a range of assembled peptides presenting the Mena EVH1 fragments that make up its discontinuous binding site for proline-rich ligands. Some of these peptides were found to inhibit the interaction of Mena EVH1 with the ligand pGolemi. One of them was further characterized at the level of individual amino acid residues; this yielded information on the contribution of individual positions of the peptides to the interaction with the ligand and identified sites for future structure optimization. [source]

Crystallization and preliminary X-ray analysis of the EVH1 domain of Vesl-2b

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2000
Melanie Barzik
Proteins of the Homer/Vesl family are enriched at excitatory synapses and selectively bind to a proline-rich consensus sequence in group 1 metabotropic glutamate receptors via a domain that shows a strong similarity to the Ena/VASP homology 1 (EVH1) domains. EVH1 domains play an important role in actin cytoskeleton dynamics. Crystals of the EVH1 domain of murine Vesl-2b were obtained that diffract X-rays to 2.4,Å resolution. They belong to space group C2, with unit-cell parameters a = 112.8, b = 69.9, c = 54.9,Å, , = 110.7°, consistent with three molecules per asymmetric unit and a solvent content of 53%. [source]