Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ZR7

Solution structure of the first WW domain of FBP11

Summary for 1ZR7
Entry DOI10.2210/pdb1zr7/pdb
NMR InformationBMRB: 6721
Descriptorhuntingtin-interacting protein HYPA/FBP11 (1 entity in total)
Functional Keywordsbeta sheet, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, signaling protein
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight3612.76
Authors
Kato, Y.,Hino, Y.,Tanokura, M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-05-19, release date: 2006-05-30, Last modification date: 2024-05-29)
Primary citationKato, Y.,Hino, Y.,Nagata, K.,Tanokura, M.
Solution structure and binding specificity of FBP11/HYPA WW domain as Group-II/III
Proteins, 63:227-234, 2006
Cited by
PubMed Abstract: The Group-II/III WW domains bind Pro-rich sequences, the most frequent protein motif found in eucaryotic genomes. We have proposed that the Group-II and -III WW domains be merged into a larger group because the members of each group have relatively wide specificity and bind to the common ligands [Kato et al., J Biol Chem 2004;279:31833-31841]. We have also proposed that Group-II/III has a common surface patch, the XP2 groove, to bind the ligands. The first WW domain of FBP11/HYPA is one of the Group-II/III WW domains. The solution structure of the 26 residue-long converged region exhibits an antiparallel triple stranded beta-sheet with a small hydrophobic core. The WW domain of FBP11/HYPA has both XP and XP2 grooves on its surface. Ligand titration by 1H-15N HSQC NMR spectra revealed that the WW domain of FBP11/HYPA binds all the peptides with the PL, PP, and PR motifs. The profile patterns of chemical shift perturbation were quite similar among the spectra titrated with all three ligands. In addition, the titration significantly shifts the signals of the residues that compose the XP2 groove. All these findings suggest the functional importance of the XP2 groove and group definition of Group-II/III of the WW domains.
PubMed: 16463264
DOI: 10.1002/prot.20880
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon