4REX
Crystal structure of the first WW domain of human YAP2 isoform
Summary for 4REX
| Entry DOI | 10.2210/pdb4rex/pdb |
| Descriptor | Yorkie homolog, SULFATE ION (3 entities in total) |
| Functional Keywords | ww domain, hippo signaling pathway, antiparallel beta-sheet, protein binding, proline rich motifs |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P46937 |
| Total number of polymer chains | 1 |
| Total formula weight | 5625.24 |
| Authors | Camara-Artigas, A. (deposition date: 2014-09-24, release date: 2015-08-19, Last modification date: 2023-09-20) |
| Primary citation | Martinez-Rodriguez, S.,Bacarizo, J.,Luque, I.,Camara-Artigas, A. Crystal structure of the first WW domain of human YAP2 isoform. J.Struct.Biol., 191:381-387, 2015 Cited by PubMed 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 1.6 Å 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. PubMed: 26256245DOI: 10.1016/j.jsb.2015.08.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
