Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain.
WW domains are small protein-protein interaction modules that recognize proline-rich stretches in proteins. The class II tandem WW domains of the formin binding protein 11 (FBP11) recognize specifically proteins containing PPLPp motifs as present in the formins that are involved in limb and kidney development, and in the methyl-CpG-binding protein 2 (MeCP2), associated with the Rett syndrome. The interaction involves the specific recognition of a leucine side-chain. Here, we report on the novel structure of the complex formed by the FPB11WW1 domain and the formin fragment APPTPPPLPP revealing the specificity determinants of class II WW domains.
Pires
José Ricardo
JR
Departamento de Bioquímica Médica, Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Trompowiski s/n CCS, Rio de Janeiro, RJ 21941-590, Brazil. jrmpires@gmx.net
Parthier
Christoph
C
Aido-Machado
Rodolpho do
Rd
Wiedemann
Urs
U
Otte
Livia
L
Böhm
Gerald
G
Rudolph
Rainer
R
Oschkinat
Hartmut
H
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018604:Epitope Mapping; D005326:Fetal Proteins / Q000737:chemistry* / Q000378:metabolism*; D000080865:Formins; D006801:Humans; D008024:Ligands; D008840:Microfilament Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013816:Thermodynamics
D002352:Carrier Proteins; D005326:Fetal Proteins; D000080865:Formins; D008024:Ligands; D008840:Microfilament Proteins; D009687:Nuclear Proteins; D010455:Peptides