8YBC
Crystal structure of coiled coil domain of Golm1 (Golgi membrane protein 1)
Summary for 8YBC
| Entry DOI | 10.2210/pdb8ybc/pdb |
| Descriptor | Golgi membrane protein 1 (2 entities in total) |
| Functional Keywords | tetramer, coiled coil, alpha-helix, oncoprotein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 32572.75 |
| Authors | |
| Primary citation | Bai, W.,Li, B.,Wu, P.,Li, X.,Huang, X.,Shi, N.,Yang, C.,Hu, F.,Xie, X. The first structure of human Golm1 coiled coil domain reveals an unexpected tetramer and highlights its structural diversity. Int.J.Biol.Macromol., 275:133624-133624, 2024 Cited by PubMed Abstract: Golgi membrane protein 1 (Golm1), a transmembrane protein with diverse subcellular localizations, has garnered significant attention in recent years due to its strong association with the development and progression of liver diseases and numerous cancers. Interestingly, although Golm1 is a membrane protein, the C-terminal of Golm1, which contains a coiled coil domain and a flexible acid region, can also be detected in the plasma of patients with various liver diseases. Notably, the coiled coil domain of serum Golm1 is postulated to play a pivotal role in physiological and pathological functions. However, little is currently known about the structure of this coiled coil domain and the full-length protein, which may limit our understanding of Golm1. Therefore, this study aims to address this gap in knowledge and reports the first crystal structure of the coiled coil domain of Golm1 at a resolution of 2.28 Å. Meanwhile, we have also confirmed that the Golm1 coiled coil domain in solution can form tetramer. Our results reveal that Golm1 can form a novel tetrameric structure that differs from the previous reported dimeric structure Golm1 could assemble, which may provide novel insights into the diversity of physiological functions and pathological roles. PubMed: 38964685DOI: 10.1016/j.ijbiomac.2024.133624 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
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