PnIA [A10L,D14K,sTy15Y] (P00505) Protein Card

General Information
Name PnIA [A10L,D14K,sTy15Y]
Alternative name(s) PnIA [A10L,D14K]
Organism synthetic construct
Protein Type Synthetic
Parent PnIA
Notes

By comparing the structures of α-conotoxins in complex with Ac-AChBP and by modelling α-conotoxins in complex with nAChRs, Lin et al. (2016) indicated that (i) Asn-11 and Asn-12 are key residues for binding to Ac-AChBP; (ii) Ser-4 is important for interaction with the Ac-AChBP complementary side; (iii) Leu-10 is responsible for the selectivity for the Ac-AChBP complementary side.


Classification
Conopeptide class conotoxin
Gene superfamily
Cysteine framework I
Pharmacological family alpha conotoxin

Sequence
GCCSLPPCALNNPKYC(nh2)
Modified residues
positionsymbolname
17nh2C-term amidation
Average Mass 1677.98
Monoisotopic Mass 1676.69
Isoelectric Point 10.45
Extinction Coefficient [280nm] 1490.00

References
Celie,P.H., Kasheverov,I.E., Mordvintsev,D.Y., Hogg,R.C., van Nierop,P., van Elk,R., van Rossum-Fikkert,S.E., Zhmak,M.N., Bertrand,D., Tsetlin,V., Sixma,T.K. and Smit,A.B. (2005) Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant Nat. Struct. Mol. Biol. 12:582-588
Lin,B., Xiang,S., and Li,M. (2016) Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs. Marine drugs 14:173

Internal links
Nucleic acids
Structure CRYSTAL STRUCTURE OF ACETYLCHOLINE-BINDING PROTEIN (ACHBP) FROM APLYSIA CALIFORNICA IN COMPLEX WITH AN ALPHA- CONOTOXIN PNIA VARIANT

External links
Ncbi 2BR8_F

Tools