1QDP
SOLUTION STRUCTURE OF ROBUSTOXIN, THE LETHAL NEUROTOXIN FROM THE FUNNEL WEB SPIDER ATRAX ROBUSTUS, NMR, 20 STRUCTURES
Summary for 1QDP
| Entry DOI | 10.2210/pdb1qdp/pdb |
| Descriptor | ROBUSTOXIN (1 entity in total) |
| Functional Keywords | neurotoxin, atrax robustus, robustoxin, cystine knot, inhibitor cystine knot motif, sodium channel modulator, funnel web spider, venom |
| Biological source | Atrax robustus |
| Cellular location | Secreted: P01478 |
| Total number of polymer chains | 1 |
| Total formula weight | 4863.75 |
| Authors | Pallaghy, P.K.,Alewood, D.,Alewood, P.F.,Norton, R.S. (deposition date: 1997-10-09, release date: 1998-01-14, Last modification date: 2024-11-20) |
| Primary citation | Pallaghy, P.K.,Alewood, D.,Alewood, P.F.,Norton, R.S. Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus. FEBS Lett., 419:191-196, 1997 Cited by PubMed Abstract: The solution structure of robustoxin, the lethal neurotoxin from the Sydney funnel-web spider Atrax robustus, has been determined from 2D 1H NMR data. Robustoxin is a polypeptide of 42 residues cross-linked by four disulphide bonds, the connectivities of which were determined from NMR data and trial structure calculations to be 1-15, 8-20, 14-31 and 16-42 (a 1-4/2-6/3-7/5-8 pattern). The structure consists of a small three-stranded, anti-parallel beta-sheet and a series of interlocking gamma-turns at the C-terminus. It also contains a cystine knot, thus placing it in the inhibitor cystine knot motif family of structures, which includes the omega-conotoxins and a number of plant and animal toxins and protease inhibitors. Robustoxin contains three distinct charged patches on its surface, and an extended loop that includes several aromatic and non-polar residues. Both of these structural features may play a role in its binding to the voltage-gated sodium channel. PubMed: 9428632DOI: 10.1016/S0014-5793(97)01452-X PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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