Structural highlights
Function
3SIMA_DENPO Selectively binds with high-affinity to the a2B-adrenoceptor subtype (ADRA2B) (PubMed:20466015). The toxin reversibly binds to ADRA2B, and its mode of inhibition is non-competitive (PubMed:20466015). The toxin has also been described to bind with high affinity to all muscarinic receptor subtypes (Ki=23 nM (on CHRM1), Ki=44 nM (on CHRM2), Ki=3 nM (on CHRM3), Ki=5 nM (on CHRM4), and Ki=8 nM (on CHRM5)) but no other data support these affinity values (PubMed:8536706).[1] [2] [3] [4]
References
- ↑ Jolkkonen M, Oras A, Toomela T, Karlsson E, Järv J, Akerman KE. Kinetic evidence for different mechanisms of interaction of black mamba toxins MT alpha and MT beta with muscarinic receptors. Toxicon. 2001 Feb-Mar;39(2-3):377-82. PMID:10978757 doi:10.1016/s0041-0101(00)00141-0
- ↑ Koivula K, Rondinelli S, Näsman J. The three-finger toxin MTalpha is a selective alpha(2B)-adrenoceptor antagonist. Toxicon. 2010 Sep 1;56(3):440-7. PMID:20466015 doi:10.1016/j.toxicon.2010.05.001
- ↑ Nareoja K, Kukkonen JP, Rondinelli S, Toivola DM, Meriluoto J, Nasman J. Adrenoceptor activity of muscarinic toxins identified from mamba venoms. Br J Pharmacol. 2011 Sep;164(2b):538-50. doi: 10.1111/j.1476-5381.2011.01468.x. PMID:21557730 doi:https://dx.doi.org/10.1111/j.1476-5381.2011.01468.x
- ↑ Jolkkonen M, Van Giersbergen PL, Hellman U, Wernstedt C, Oras A, Satyapan N, Adem A, Karlsson E. Muscarinic toxins from the black mamba Dendroaspis polylepis. Eur J Biochem. 1995 Dec 1;234(2):579-85. PMID:8536706 doi:10.1111/j.1432-1033.1995.579_b.x
