2LOS
Backbone structure of human membrane protein TMEM14C
Summary for 2LOS
| Entry DOI | 10.2210/pdb2los/pdb |
| Related | 2LOM 2LON 2LOO 2LOP 2LOQ 2LOR |
| NMR Information | BMRB: 18223 |
| Descriptor | Transmembrane protein 14C (1 entity in total) |
| Functional Keywords | membrane protein, paramagnetic relaxation enhancement, helical bundle |
| Biological source | Homo sapiens (human) |
| Cellular location | Mitochondrion membrane; Multi-pass membrane protein (By similarity): Q9P0S9 |
| Total number of polymer chains | 1 |
| Total formula weight | 12613.80 |
| Authors | Klammt, C.,Vajpai, N.,Maslennikov, I.,Riek, R.,Choe, S. (deposition date: 2012-01-26, release date: 2012-05-23, Last modification date: 2024-05-15) |
| Primary citation | Klammt, C.,Maslennikov, I.,Bayrhuber, M.,Eichmann, C.,Vajpai, N.,Chiu, E.J.,Blain, K.Y.,Esquivies, L.,Kwon, J.H.,Balana, B.,Pieper, U.,Sali, A.,Slesinger, P.A.,Kwiatkowski, W.,Riek, R.,Choe, S. Facile backbone structure determination of human membrane proteins by NMR spectroscopy. Nat.Methods, 9:834-839, 2012 Cited by PubMed Abstract: Although nearly half of today's major pharmaceutical drugs target human integral membrane proteins (hIMPs), only 30 hIMP structures are currently available in the Protein Data Bank, largely owing to inefficiencies in protein production. Here we describe a strategy for the rapid structure determination of hIMPs, using solution NMR spectroscopy with systematically labeled proteins produced via cell-free expression. We report new backbone structures of six hIMPs, solved in only 18 months from 15 initial targets. Application of our protocols to an additional 135 hIMPs with molecular weight <30 kDa yielded 38 hIMPs suitable for structural characterization by solution NMR spectroscopy without additional optimization. PubMed: 22609626DOI: 10.1038/nmeth.2033 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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