메뉴 건너뛰기




Volumn 7, Issue 1, 2015, Pages 34-42

Plectasin, first animal Toxin-Like fungal defensin blocking potassium channels through recognizing channel pore region

Author keywords

Defensin; Functional evolution; Kv1.3 channel; Molecular mechanism; Plectasin; Potassium channels

Indexed keywords

CHARYBDOTOXIN; PLECTASIN; POTASSIUM CHANNEL HERG; POTASSIUM CHANNEL KCNQ; POTASSIUM CHANNEL KV1.1; POTASSIUM CHANNEL KV1.2; SCORPION VENOM; DEFENSIN; MYCOTOXIN; PEPTIDE; POTASSIUM CHANNEL; POTASSIUM CHANNEL BLOCKING AGENT;

EID: 84921743972     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins7010034     Document Type: Article
Times cited : (28)

References (27)
  • 1
    • 0033635776 scopus 로고    scopus 로고
    • Potassium channels: Molecular defects, diseases, and therapeutic opportunities
    • Shieh, C.C.; Coghlan, M.; Sullivan, J.P.; Gopalakrishnan, M. Potassium channels: Molecular defects, diseases, and therapeutic opportunities. Pharmacol. Rev. 2000, 52, 557-594.
    • (2000) Pharmacol. Rev , vol.52 , pp. 557-594
    • Shieh, C.C.1    Coghlan, M.2    Sullivan, J.P.3    Gopalakrishnan, M.4
  • 2
  • 3
    • 84877106599 scopus 로고    scopus 로고
    • Two conserved arginine residues from the SK3 potassium channel outer vestibule control selectivity of recognition by scorpion toxins
    • Feng, J.; Hu, Y.; Yi, H.; Yin, S.; Han, S.; Hu, J.; Chen, Z.; Yang, W.; Cao, Z.; de Waard, M.; et al. Two conserved arginine residues from the SK3 potassium channel outer vestibule control selectivity of recognition by scorpion toxins. J. Biol. Chem. 2013, 288, 12544-12553.
    • (2013) J. Biol. Chem , vol.288 , pp. 12544-12553
    • Feng, J.1    Hu, Y.2    Yi, H.3    Yin, S.4    Han, S.5    Hu, J.6    Chen, Z.7    Yang, W.8    Cao, Z.9    de Waard, M.10
  • 4
    • 84865476388 scopus 로고    scopus 로고
    • − effector memory T cell activation by a novel peptide targeting Kv1.3 channel in a rat experimental autoimmune encephalomyelitis model
    • − effector memory T cell activation by a novel peptide targeting Kv1.3 channel in a rat experimental autoimmune encephalomyelitis model. J. Biol. Chem. 2012, 287, 29479-29494.
    • (2012) J. Biol. Chem , vol.287 , pp. 29479-29494
    • Li, Z.1    Liu, W.H.2    Han, S.3    Peng, B.W.4    Yin, J.5    Wu, Y.L.6    He, X.H.7    Li, W.X.8
  • 6
    • 84893120991 scopus 로고    scopus 로고
    • Free energy simulations of binding of HsTx1 toxin to Kv1 potassium channels: The basis of Kv1.3/Kv1.1 selectivity
    • Rashid, M.H.; Kuyucak, S. Free energy simulations of binding of HsTx1 toxin to Kv1 potassium channels: The basis of Kv1.3/Kv1.1 selectivity. J. Phys. Chem. B 2014, 118, 707-716.
    • (2014) J. Phys. Chem. B , vol.118 , pp. 707-716
    • Rashid, M.H.1    Kuyucak, S.2
  • 7
    • 35248857005 scopus 로고    scopus 로고
    • Molecular mechanism of the sea anemone toxin ShK recognizing the Kv1.3 channel explored by docking and molecular dynamic simulations
    • Jin, L.; Wu, Y. Molecular mechanism of the sea anemone toxin ShK recognizing the Kv1.3 channel explored by docking and molecular dynamic simulations. J. Chem. Inf. Model. 2007, 47, 1967-1972.
    • (2007) J. Chem. Inf. Model , vol.47 , pp. 1967-1972
    • Jin, L.1    Wu, Y.2
  • 8
    • 82955194460 scopus 로고    scopus 로고
    • Modeling the binding of three toxins to the voltage-gated potassium channel (Kv1.3)
    • Chen, R.; Robinson, A.; Gordon, D.; Chung, S.H. Modeling the binding of three toxins to the voltage-gated potassium channel (Kv1.3). Biophys. J. 2011, 101, 2652-2660.
    • (2011) Biophys. J , vol.101 , pp. 2652-2660
    • Chen, R.1    Robinson, A.2    Gordon, D.3    Chung, S.H.4
  • 9
    • 84860307772 scopus 로고    scopus 로고
    • Affinity and selectivity of ShK toxin for the Kv1 potassium channels from free energy simulations
    • Rashid, M.H.; Kuyucak, S. Affinity and selectivity of ShK toxin for the Kv1 potassium channels from free energy simulations. J. Phys. Chem. B 2012, 116, 4812-4822.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 4812-4822
    • Rashid, M.H.1    Kuyucak, S.2
  • 10
    • 4444295137 scopus 로고    scopus 로고
    • Differential antifungal and calcium channel-blocking activity among structurally related plant defensins
    • Spelbrink, R.G.; Dilmac, N.; Allen, A.; Smith, T.J.; Shah, D.M.; Hockerman, G.H. Differential antifungal and calcium channel-blocking activity among structurally related plant defensins. Plant Physiol. 2004, 135, 2055-2067.
    • (2004) Plant Physiol , vol.135 , pp. 2055-2067
    • Spelbrink, R.G.1    Dilmac, N.2    Allen, A.3    Smith, T.J.4    Shah, D.M.5    Hockerman, G.H.6
  • 11
    • 84888239118 scopus 로고    scopus 로고
    • Antimicrobial activity of defensins and defensin-like peptides with special emphasis on those from fungi and invertebrate animals
    • Ng, T.B.; Cheung, R.C.; Wong, J.H.; Ye, X.J. Antimicrobial activity of defensins and defensin-like peptides with special emphasis on those from fungi and invertebrate animals. Curr. Protein Pept. Sci. 2013, 14, 515-531.
    • (2013) Curr. Protein Pept. Sci , vol.14 , pp. 515-531
    • Ng, T.B.1    Cheung, R.C.2    Wong, J.H.3    Ye, X.J.4
  • 13
    • 84918524333 scopus 로고    scopus 로고
    • Sequence diversity and evolution of antimicrobial peptides in invertebrates
    • Tassanakajon, A.; Somboonwiwat, K.; Amparyup, P. Sequence diversity and evolution of antimicrobial peptides in invertebrates. Dev. Comp. Immunol. 2015, 48, 324-341.
    • (2015) Dev. Comp. Immunol , vol.48 , pp. 324-341
    • Tassanakajon, A.1    Somboonwiwat, K.2    Amparyup, P.3
  • 14
    • 84925487807 scopus 로고    scopus 로고
    • Endogenous animal toxin-like human beta-defensin 2 inhibits own K channels through interaction with channel extracellular pore region
    • Yang, W.; Feng, J.; Xiang, F.; Xie, Z.; Zhang, G.; Sabatier, J.M.; Cao, Z.; Li, W.; Chen, Z.; Wu, Y. Endogenous animal toxin-like human beta-defensin 2 inhibits own K channels through interaction with channel extracellular pore region. Cell. Mol. Life Sci. 2014, doi:10.1007/s00018-014-1715-z.
    • (2014) Cell. Mol. Life Sci
    • Yang, W.1    Feng, J.2    Xiang, F.3    Xie, Z.4    Zhang, G.5    Sabatier, J.M.6    Cao, Z.7    Li, W.8    Chen, Z.9    Wu, Y.10
  • 18
    • 53049107758 scopus 로고    scopus 로고
    • Structural basis for toxin resistance of beta4-associated calcium-activated potassium (BK) channels
    • Gan, G.; Yi, H.; Chen, M.; Sun, L.; Li, W.; Wu, Y.; Ding, J. Structural basis for toxin resistance of beta4-associated calcium-activated potassium (BK) channels. J. Biol. Chem. 2008, 283, 24177-24184.
    • (2008) J. Biol. Chem , vol.283 , pp. 24177-24184
    • Gan, G.1    Yi, H.2    Chen, M.3    Sun, L.4    Li, W.5    Wu, Y.6    Ding, J.7
  • 19
    • 68149156012 scopus 로고    scopus 로고
    • Molecular Information of charybdotoxin blockade in the large conductance calcium-activated potassium channel
    • Qiu, S.; Yi, H.; Liu, H.; Cao, Z.; Wu, Y.; Li, W. Molecular Information of charybdotoxin blockade in the large conductance calcium-activated potassium channel. J. Chem. Inf. Model. 2009, 49, 1831-1838.
    • (2009) J. Chem. Inf. Model , vol.49 , pp. 1831-1838
    • Qiu, S.1    Yi, H.2    Liu, H.3    Cao, Z.4    Wu, Y.5    Li, W.6
  • 21
    • 49649113677 scopus 로고    scopus 로고
    • Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease
    • Han, S.; Yi, H.; Yin, S.J.; Chen, Z.Y.; Liu, H.; Cao, Z.J.; Wu, Y.L.; Li, W.X. Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease. J. Biol. Chem. 2008, 283, 19058-19065.
    • (2008) J. Biol. Chem , vol.283 , pp. 19058-19065
    • Han, S.1    Yi, H.2    Yin, S.J.3    Chen, Z.Y.4    Liu, H.5    Cao, Z.J.6    Wu, Y.L.7    Li, W.X.8
  • 22
    • 58149377754 scopus 로고    scopus 로고
    • Different residues in channel turret determining the selectivity of ADWX-1 inhibitor peptide between Kv1.1 and Kv1.3 channels
    • Yin, S.J.; Jiang, L.; Yi, H.; Han, S.; Yang, D.W.; Liu, M.L.; Liu, H.; Cao, Z.J.; Wu, Y.L.; Li, W.X. Different residues in channel turret determining the selectivity of ADWX-1 inhibitor peptide between Kv1.1 and Kv1.3 channels. J. Proteome Res. 2008, 7, 4890-4897.
    • (2008) J. Proteome Res , vol.7 , pp. 4890-4897
    • Yin, S.J.1    Jiang, L.2    Yi, H.3    Han, S.4    Yang, D.W.5    Liu, M.L.6    Liu, H.7    Cao, Z.J.8    Wu, Y.L.9    Li, W.X.10
  • 24
    • 84859984930 scopus 로고    scopus 로고
    • Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family
    • Chen, Z.Y.; Hu, Y.T.; Yang, W.S.; He, Y.W.; Feng, J.; Wang, B.; Zhao, R.M.; Ding, J.P.; Cao, Z.J.; Li, W.X.; et al. Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family. J. Biol. Chem. 2012, 287, 13813-13821.
    • (2012) J. Biol. Chem , vol.287 , pp. 13813-13821
    • Chen, Z.Y.1    Hu, Y.T.2    Yang, W.S.3    He, Y.W.4    Feng, J.5    Wang, B.6    Zhao, R.M.7    Ding, J.P.8    Cao, Z.J.9    Li, W.X.10
  • 26
    • 84857892330 scopus 로고    scopus 로고
    • Engineering a potent and specific blocker of voltage-gated potassium channel Kv1.3, a target for autoimmune diseases
    • Chen, R.; Chung, S.H. Engineering a potent and specific blocker of voltage-gated potassium channel Kv1.3, a target for autoimmune diseases. Biochemistry 2012, 51, 1976-1982.
    • (2012) Biochemistry , vol.51 , pp. 1976-1982
    • Chen, R.1    Chung, S.H.2
  • 27
    • 84897070280 scopus 로고    scopus 로고
    • Physiological role of Kv1.3 channel in T lymphocyte cell investigated quantitatively by kinetic modeling
    • Hou, P.; Zhang, R.; Liu, Y.; Feng, J.; Wang, W.; Wu, Y.; Ding, J. Physiological role of Kv1.3 channel in T lymphocyte cell investigated quantitatively by kinetic modeling. PLoS One 2014, 9, e89975.
    • (2014) PLoS One , vol.9
    • Hou, P.1    Zhang, R.2    Liu, Y.3    Feng, J.4    Wang, W.5    Wu, Y.6    Ding, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.