2LOP

Backbone structure of human membrane protein TMEM14A

Summary for 2LOP

• Entry DOI: 10.2210/pdb2lop/pdb
• Related: 2LOM 2LON 2LOO 2LOQ
• NMR Information: BMRB: 18220
• Descriptor: Transmembrane protein 14A (1 entity in total)
• Functional Keywords: membrane protein, helical bundle
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Multi-pass membrane protein (Potential): Q9Y6G1
• Total number of polymer chains: 1
• Total formula weight: 11735.31

Authors

Eichmann, C.,Klammt, C.,Maslennikov, I.,Kwiatkowski, W.,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

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: 22609626
DOI: 10.1038/nmeth.2033

Experimental method

SOLUTION NMR