1ter

SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY

spinqualitylabelsall models 1ter, 21 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ter is a 1 chain structure with sequence from Apime. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TERT_APIME] Presynaptic neurotoxin that blocks the inwardly rectifying Kir1.1/KCNJ1 and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. It may block the potassium channel pore by occluding its alpha helix into the channel vestibule. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimers potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named I(KACh), because these channels are activated by ACh) are found in mammalian myocytes. Interacts specifically with calmodulin in the presence of calcium. Publication Abstract from PubMed The solution structure of tertiapin, a 21-residue bee venom peptide, has been characterized by circular dichroism (CD), two-dimensional nuclear magnetic resonance (NMR) spectroscopy, and distance geometry. A total of 21 lowest error structures were obtained from distance geometry calculations. Superimposition of these structures shows that the backbone of tertiapin is very well defined. One type-I reverse turn from residue 4 to 7 and an alpha-helix from residue 12 to 19 exist in the structure of tertiapin. The alpha-helical region is best defined from both conformational analysis and structural superimposition. The overall three-dimensional structure of tertiapin is highly compact resulting from side chain interactions. The structural information obtained from CD and NMR are compared for both tertiapin and apamin (ref. 3), another bee venom peptide. Tertiapin and apamin have some similar secondary structure, but display different tertiary structures. Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry.,Xu X, Nelson JW Proteins. 1993 Oct;17(2):124-37. PMID:8265561 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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