2N7Y
NMR structure of metal-binding domain 1 of ATP7B
Summary for 2N7Y
| Entry DOI | 10.2210/pdb2n7y/pdb |
| Descriptor | Copper-transporting ATPase 2 (1 entity in total) |
| Functional Keywords | copper binding, hydrolase, metal binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Golgi apparatus, trans-Golgi network membrane ; Multi- pass membrane protein . Isoform 1: Golgi apparatus membrane ; Multi-pass membrane protein . Isoform 2: Cytoplasm . WND/140 kDa: Mitochondrion : P35670 |
| Total number of polymer chains | 1 |
| Total formula weight | 8122.46 |
| Authors | Yu, C.,Lee, W.,Dmitriev, O. (deposition date: 2015-09-27, release date: 2016-09-28, Last modification date: 2024-05-15) |
| Primary citation | Yu, C.H.,Lee, W.,Nokhrin, S.,Dmitriev, O.Y. The Structure of Metal Binding Domain 1 of the Copper Transporter ATP7B Reveals Mechanism of a Singular Wilson Disease Mutation. Sci Rep, 8:581-581, 2018 Cited by PubMed Abstract: Copper-transporter ATP7B maintains copper homeostasis in the human cells and delivers copper to the biosynthetic pathways for incorporation into the newly synthesized copper-containing proteins. ATP7B is a target of several hundred mutations that lead to Wilson disease, a chronic copper toxicosis. ATP7B contains a chain of six cytosolic metal-binding domains (MBDs), the first four of which (MBD1-4) are believed to be regulatory, and the last two (MBD5-6) are required for enzyme activity. We report the NMR structure of MBD1, the last unsolved metal-binding domain of ATP7B. The structure reveals the disruptive mechanism of G85V mutation, one of the very few disease causing missense mutations in the MBD1-4 region of ATP7B. PubMed: 29330485DOI: 10.1038/s41598-017-18951-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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