PDBsum entry 4rex

Protein binding

PDB id: 4rex

Contents

Protein chain

48 a.a.

Ligands

SO4

Waters ×42

PDB id:

4rex

Name:

Protein binding

Title:

Crystal structure of the first ww domain of human yap2 isoform

Structure:

Yorkie homolog. Chain: a. Fragment: ww domain (unp residues 165-209). Synonym: 65 kda yes-associated protein, yap65. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: yap1, yap65. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.60Å R-factor: 0.179 R-free: 0.194

Authors:

A.Camara-Artigas

Key ref:

S.Martinez-Rodriguez et al. (2015). Crystal structure of the first WW domain of human YAP2 isoform. J Struct Biol, 191, 381-387. PubMed id: 26256245 DOI: 10.1016/j.jsb.2015.08.001

Date:

24-Sep-14 Release date: 19-Aug-15

Protein chain

P46937  (YAP1_HUMAN) -  Transcriptional coactivator YAP1 from Homo sapiens

Seq: 504 a.a.

Struc: 48 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

DOI no: 10.1016/j.jsb.2015.08.001

J Struct Biol 191:381-387 (2015)

PubMed id: 26256245

Crystal structure of the first WW domain of human YAP2 isoform.

S.Martinez-Rodriguez, J.Bacarizo, I.Luque, A.Camara-Artigas.

ABSTRACT

The WW domains are the smallest modular domains known. The study of the structural basis of their stability is important to understand their physiological role. These domains are intrinsically flexible, which makes them difficult to crystallize. The first WW domain of the human Yes tyrosine kinase Associated Protein (YAP) has been crystallized and its structure has been solved by X-ray diffraction at 1.6Å resolution. Crystals belong to the orthorhombic space group P21212 with unit cell parameters a=42.67, b=43.10 and c=21.30. The addition of proline and other small-molecule additives improves drastically the quality of the crystals. The interactions that stabilize this minimal modular domain have been analysed. This crystal structure reveals that, besides the stabilization of the hydrophobic core of the protein by the aromatic cluster formed by Trp177-Phe189-Pro202, some salt-bridges interactions might affect the stability of the domain.