Article
Aromatic and basic residues within the EVH1 domain of VASP specify its interaction with proline-rich ligands.
Current biology : CB - 1 Jul 1999
Carl U D, Pollmann M, Orr E, Gertlere F B, Chakraborty T, Wehland J
Abstract excerpt
Short contiguous peptides harboring proline-rich motifs are frequently involved in protein-protein interactions, such as associations with Src homology 3 (SH3) and WW domains. Although patches of aromatic residues present in either domain interact with polyprolines, their overall structures are distinct, suggesting that additional protein families exist that use stacked aromatic amino acids (AA domains) to bind...
Topics
- Amino Acid Sequence
- Animals
- Bacterial Proteins
- Carrier Proteins
- Cell Adhesion Molecules
- Cell Line
- Conserved Sequence
- Cytoskeletal Proteins
- Drosophila
- Listeria monocytogenes
- Membrane Proteins
- Mice
- Microfilament Proteins
- Molecular Sequence Data