1BCG
SCORPION TOXIN BJXTR-IT
Summary for 1BCG
Entry DOI | 10.2210/pdb1bcg/pdb |
Descriptor | TOXIN BJXTR-IT (2 entities in total) |
Functional Keywords | excitatory neurotoxin |
Biological source | Hottentotta judaicus |
Cellular location | Secreted: P56637 |
Total number of polymer chains | 1 |
Total formula weight | 8597.83 |
Authors | Oren, D.,Froy, O.,Amit, E.,Kleinberger-Doron, N.,Gurevitz, M.,Shaanan, B. (deposition date: 1998-04-29, release date: 1998-11-18, Last modification date: 2024-10-30) |
Primary citation | Oren, D.A.,Froy, O.,Amit, E.,Kleinberger-Doron, N.,Gurevitz, M.,Shaanan, B. An excitatory scorpion toxin with a distinctive feature: an additional alpha helix at the C terminus and its implications for interaction with insect sodium channels. Structure, 6:1095-1103, 1998 Cited by PubMed Abstract: Scorpion neurotoxins, which bind and modulate sodium channels, have been divided into two groups, the alpha and beta toxins, according to their activities. The beta-toxin class includes the groups of excitatory and depressant toxins, which differ in their mode of action and are highly specific against insects. The three-dimensional structures of several alpha and beta toxins have been determined at high resolution, but no detailed 3D structure of an excitatory toxin has been presented so far. PubMed: 9753689DOI: 10.1016/S0969-2126(98)00111-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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