1LIR
LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES
Summary for 1LIR
Entry DOI | 10.2210/pdb1lir/pdb |
Descriptor | LQ2 (1 entity in total) |
Functional Keywords | neurotoxin, scorpion, potassium channel blocker, inward rectifier potassium channel |
Biological source | Leiurus quinquestriatus hebraeus |
Total number of polymer chains | 1 |
Total formula weight | 4350.02 |
Authors | Renisio, J.G.,Lu, Z.,Blanc, E.,Jin, W.,Lewis, J.H.,Bornet, O.,Darbon, H. (deposition date: 1998-04-02, release date: 1998-06-17, Last modification date: 2024-11-13) |
Primary citation | Renisio, J.G.,Lu, Z.,Blanc, E.,Jin, W.,Lewis, J.H.,Bornet, O.,Darbon, H. Solution structure of potassium channel-inhibiting scorpion toxin Lq2. Proteins, 34:417-426, 1999 Cited by PubMed Abstract: Lq2 is a unique scorpion toxin. Acting from the extracellular side, Lq2 blocks the ion conduction pore in not only the voltage- and Ca2+ -activated channels, but also the inward-rectifier K+ channels. This finding argues that the three-dimensional structures of the pores in these K+ channels are similar. However, the amino acid sequences that form the external part of the pore are minimally conserved among the various classes of K+ channels. Because Lq2 can bind to all the three classes of K+ channels, we can use Lq2 as a structural probe to examine how the non-conserved pore-forming sequences are arranged in space to form similar pore structures. In the present study, we determined the three-dimensional structure of Lq2 using nuclear magnetic resonance (NMR) techniques. Lq2 consists of an alpha-helix (residues S10 to L20) and a beta-sheet, connected by an alphabeta3 loop (residues N22 to N24). The beta-sheet has two well-defined anti-parallel strands (residues G26 to M29 and residues K32 to C35), which are connected by a type I' beta-turn centered between residues N30 and K31. The N-terminal segment (residues Z1 to T8) appears to form a quasi-third strand of the beta-sheet. PubMed: 10081954DOI: 10.1002/(SICI)1097-0134(19990301)34:4<417::AID-PROT1>3.3.CO;2-I PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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