WW and SH3 domains, two different scaffolds to recognize proline-rich ligands.
WW domains are small protein modules composed of approximately 40 amino acids. These domains fold as a stable, triple stranded beta-sheet and recognize proline-containing ligands. WW domains are found in many different signaling and structural proteins, often localized in the cytoplasm as well as in the cell nucleus. Based on analyses of seven structures of WW domains, we discuss their diverse binding preferences and sequence conservation patterns. While modeling WW domains for which structures have not been determined we uncovered a case of potential molecular and functional convergence between WW and SH3 domains. The binding surface of the modeled WW domain of Npw38 protein shows a remarkable similarity to the SH3 domain of Sem5 protein, confirming biochemical data on similar binding predilections of both domains.
Macias
Maria J
MJ
Structural and Computational Biology Program, EMBL Heidelberg, Heidelberg, Germany. macias@embl-heidelberg.de
Wiesner
Silke
S
Sudol
Marius
M
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D008024:Ligands; D008969:Molecular Sequence Data; D011392:Proline; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D018909:src Homology Domains
D008024:Ligands; D011392:Proline