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1LIR

LQ2 FROM LEIURUS QUINQUESTRIATUS, NMR, 22 STRUCTURES

Summary for 1LIR
Entry DOI10.2210/pdb1lir/pdb
DescriptorLQ2 (1 entity in total)
Functional Keywordsneurotoxin, scorpion, potassium channel blocker, inward rectifier potassium channel
Biological sourceLeiurus quinquestriatus hebraeus
Total number of polymer chains1
Total formula weight4350.02
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 citationRenisio, 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: 10081954
DOI: 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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