PDBsum entry 1zr7

Signaling protein

PDB id: 1zr7

Contents

Protein chain

30 a.a. *

* Residue conservation analysis

PDB id:

1zr7

Name:

Signaling protein

Title:

Solution structure of the first ww domain of fbp11

Structure:

Huntingtin-interacting protein hypa/fbp11. Chain: a. Fragment: residues in database 150-177. Synonym: formin binding protein 11 (fbp11)/huntingtin yeast partner a (hypa). Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: fbp11. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

Y.Kato,Y.Hino,M.Tanokura,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

Y.Kato et al. (2006). Solution structure and binding specificity of FBP11/HYPA WW domain as Group-II/III. Proteins, 63, 227-234. PubMed id: 16463264 DOI: 10.1002/prot.20880

Date:

19-May-05 Release date: 30-May-06

Protein chain

O75400  (PR40A_HUMAN) -  Pre-mRNA-processing factor 40 homolog A from Homo sapiens

Seq: 957 a.a.

Struc: 30 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1002/prot.20880

Proteins 63:227-234 (2006)

PubMed id: 16463264

Solution structure and binding specificity of FBP11/HYPA WW domain as Group-II/III.

Y.Kato, Y.Hino, K.Nagata, M.Tanokura.

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.

Selected figure(s)

Figure 1.
Figure 1. Solution structure of FBP11 WW1. Superimposition of the best 20 structures out of 100 calculated structures of FBP11 WW1 from CYANA-2.0.

Figure 2.
Figure 2. Comparison of FBP11 WW1 to other Group-II/III WW domains. (A) Alignment of four WW domains that are similar to FBP11 WW1. The red characters show completely identical residues among these four proteins. We used residue numbering that we had defined previously to facilitate the comparison to other WW domains.[4] Based on this residue numbering system, we numbered the second Trp the 34th residue, which is the 168th in the entire FBP11/HYPA sequence. The arrows show the positions of the -strands that were predicted by CSI.[21] The intervals between strands were referred to as Loops I and II. (B) Superposition of backbones of the Group-II/III WW domains published so far, including the side chains of Trp12, Tyr24, and Pro37. The orange, pink, blue, and green bonds are the NMR mean structures of FBP11 WW1 by Pires and colleagues (PDB code: 1YWJ), FBP11 WW1 by the present authors (PDB code: 1ZR7), FBP28 WW2 (PDB code: 1E0L), and Prp40 WW1 (PDB code: 1O6W), respectively,[25][26] corresponding to the font colors in (A). The side chain of Pro18 of FBP11 WW1 was additionally depicted. The two sides of the WW domain sheet structure were defined, which are referred to as the binding side and backside. The drawing and fitting of the molecules were carried out with Swiss PDB viewer.[31] (C) Superposition of the backbones of the FBP11 WW1 structures by Pires and colleagues and the present authors from the different orientation from that in (B). The color code is the same as (B).

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 63, 227-234) copyright 2006.

Figures were selected by an automated process.