5NDA
NMR Structural Characterisation of Pharmaceutically Relevant Proteins Obtained Through a Novel Recombinant Production: The Case of The Pulmonary Surfactant Polypeptide C Analogue rSP-C33Leu.
Summary for 5NDA
| Entry DOI | 10.2210/pdb5nda/pdb |
| NMR Information | BMRB: 34114 |
| Descriptor | rSP-C33Leu -RECOMBINANT PULMONARY SURFACTANT-ASSOCIATED POLYPEPTIDE C ANALOGUE- (1 entity in total) |
| Functional Keywords | protein, pulmonary surfactant protein, sp-c analogue, recombinant protein, solubility tag, fusion protein, nt domain, protein structure |
| Biological source | Sus scrofa (Pig) |
| Total number of polymer chains | 1 |
| Total formula weight | 3600.73 |
| Authors | Venturi, L.,Pioselli, B.,Johansson, J.,Rising, A.,Kronqvist, N.,Nordling, K. (deposition date: 2017-03-08, release date: 2017-06-07, Last modification date: 2024-06-19) |
| Primary citation | Kronqvist, N.,Sarr, M.,Lindqvist, A.,Nordling, K.,Otikovs, M.,Venturi, L.,Pioselli, B.,Purhonen, P.,Landreh, M.,Biverstal, H.,Toleikis, Z.,Sjoberg, L.,Robinson, C.V.,Pelizzi, N.,Jornvall, H.,Hebert, H.,Jaudzems, K.,Curstedt, T.,Rising, A.,Johansson, J. Efficient protein production inspired by how spiders make silk. Nat Commun, 8:15504-15504, 2017 Cited by PubMed Abstract: Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general. PubMed: 28534479DOI: 10.1038/ncomms15504 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
