Summary for 1Q2U
| Entry DOI | 10.2210/pdb1q2u/pdb |
| Related | 1PS4 |
| Descriptor | RNA-binding protein regulatory subunit (2 entities in total) |
| Functional Keywords | breast cancer, parkinson's disease, male fertility, protein inhibitor of activated stat, androgen receptor, rna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q99497 |
| Total number of polymer chains | 1 |
| Total formula weight | 19917.05 |
| Authors | Huai, Q.,Sun, Y.,Wang, H.,Chin, L.S.,Li, L.,Robinson, H.,Ke, H. (deposition date: 2003-07-26, release date: 2003-10-07, Last modification date: 2024-02-21) |
| Primary citation | Huai, Q.,Sun, Y.,Wang, H.,Chin, L.S.,Li, L.,Robinson, H.,Ke, H. Crystal structure of DJ-1/RS and implication on familial Parkinson's disease Febs Lett., 549:171-175, 2003 Cited by PubMed Abstract: DJ-1 is a protein involved in multiple physiological processes, including cancer, Parkinson's disease, and male fertility. It is unknown how DJ-1 functions in the apparently different systems. The crystal structure of DJ-1 at 1.6 A resolution shows that DJ-1 is a helix-strand-helix sandwich and forms a dimer. The DJ-1 structure is similar to the members of the intracellular protease PfpI family. However, the catalytic triad of Cys-His-Glu is not strictly conserved in DJ-1, implying that DJ-1 has a different catalytic mechanism if it acts as a protease or DJ-1 serves as a regulatory protein in the physiological processes. The structure shows that Leu166 positions in the middle of a helix and thus predicts that the L166P mutation will bend the helix and impact the dimerization of DJ-1. As a result, the conformational changes may diminish the DJ-1 binding with its partner, leading to the familial Parkinson's disease caused by the single L166P mutation. PubMed: 12914946DOI: 10.1016/S0014-5793(03)00764-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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