2LON
Backbone structure of human membrane protein HIGD1B
Summary for 2LON
| Entry DOI | 10.2210/pdb2lon/pdb |
| Related | 2LOM 2LOO 2LOP 2LOQ |
| NMR Information | BMRB: 18218 |
| Descriptor | HIG1 domain family member 1B (1 entity in total) |
| Functional Keywords | membrane protein, helical bundle |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Multi-pass membrane protein (Potential): Q9P298 |
| Total number of polymer chains | 1 |
| Total formula weight | 11074.96 |
| Authors | Klammt, C.,Maslennikov, I.,Kwiatkowski, W.,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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