1GD5
SOLUTION STRUCTURE OF THE PX DOMAIN FROM HUMAN P47PHOX NADPH OXIDASE
Summary for 1GD5
| Entry DOI | 10.2210/pdb1gd5/pdb |
| Descriptor | NEUTROPHIL CYTOSOL FACTOR 1 (1 entity in total) |
| Functional Keywords | alpha beta, p47-phox, px domain, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15325.80 |
| Authors | Hiroaki, H.,Ago, T.,Ito, T.,Sumimoto, H.,Kohda, D. (deposition date: 2000-09-14, release date: 2001-06-13, Last modification date: 2023-12-27) |
| Primary citation | Hiroaki, H.,Ago, T.,Ito, T.,Sumimoto, H.,Kohda, D. Solution structure of the PX domain, a target of the SH3 domain. Nat.Struct.Biol., 8:526-530, 2001 Cited by PubMed Abstract: The phox homology (PX) domain is a novel protein module containing a conserved proline-rich motif. We have shown that the PX domain isolated from the human p47phox protein, a soluble subunit of phagocyte NADPH oxidase, binds specifically to the C-terminal SH3 domain derived from the same protein. The solution structure of p47 PX has an alpha + beta structure with a novel folding motif topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proline-rich motif of p47 PX in the free state adopts a distorted left-handed polyproline type II helix conformation. PubMed: 11373621DOI: 10.1038/88591 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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