5nq4 | pdb_00005nq4

Cytotoxin-1 in DPC-micelle

spinqualitylabelsall models 5nq4 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nq4 is a 1 chain structure with sequence from Naja oxiana. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 3SA1_NAJOX This three-finger cytotoxin is a basic protein that interacts and penetrates into the cell membrane, with the tips of all the three loops. Cytotoxins which have a 'Pro-30' (P-type) interacts with membrane stronger that those which have a Ser-28 (S-type). CTI interacts with membrane weaker than CTII. Publication Abstract from PubMed Cobra cytotoxins (CTs) belong to the three-fingered protein family. They are classified into S- and P-types, the latter exhibiting higher membrane-perturbing capacity. In this work, we investigated the interaction of CTs with phospholipid bilayers, using coarse-grained (CG) and full-atom (FA) molecular dynamics (MD). The object of this work is a CT of an S-type, cytotoxin I (CT1) from N.oxiana venom. Its spatial structure in aqueous solution and in the micelles of dodecylphosphocholine (DPC) were determined by (1)H-NMR spectroscopy. Then, via CG- and FA MD-computations, we evaluated partitioning of CT1 molecule into palmitoyloleoylphosphatidylcholine (POPC) membrane, using the toxin spatial models, obtained either in aqueous solution, or detergent micelle. The latter model exhibits minimal structural changes upon partitioning into the membrane, while the former deviates from the starting conformation, loosing the tightly bound water molecule in the loop-2. These data show that the structural changes elicited by CT1 molecule upon incorporation into DPC micelle take place likely in the lipid membrane, although the mode of the interaction of this toxin with DPC micelle (with the tips of the all three loops) is different from its mode in POPC membrane (primarily with the tip of the loop-1 and both the tips of the loop-1 and loop-2). Impact of membrane partitioning on the spatial structure of an S-type cobra cytotoxin.,Dubovskii PV, Dubinnyi MA, Volynsky PE, Pustovalova YE, Konshina AG, Utkin YN, Arseniev AS, Efremov RG J Biomol Struct Dyn. 2017 Nov 6:1-16. doi: 10.1080/07391102.2017.1389662. PMID:28990854 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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