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Effect of cobratoxin binding on the normal mode vibration within acetylcholine binding protein
Stanford University.
Stockholm University.ORCID iD: 0000-0002-2734-2794
Netherlands Cancer Institute.
Stanford University.
2008 (English)In: Journal of chemical information and modeling, ISSN 1549-9596, Vol. 48, no 4, 855-860 p.Article in journal (Refereed) Published
Abstract [en]

Recent crystal structures of the acetylcholine binding protein (AChBP) have revealed surprisingly small structural alterations upon ligand binding. Here we investigate the extent to which ligand binding may affect receptor dynamics. AChBP is a homologue of the extracellular component of ligand-gated ion channels (LGICs). We have previously used an elastic network normal-mode analysis to propose a gating mechanism for the LGICs and to suggest the effects of various ligands on such motions. However, the difficulties with elastic network methods lie in their inability to account for the modest effects of a small ligand or mutation on ion channel motion. Here, we report the successful application of an elastic network normal mode technique to measure the effects of large ligand binding on receptor dynamics. The present calculations demonstrate a clear alteration in the native symmetric motions of a protein due to the presence of large protein cobratoxin ligands. In particular, normal-mode analysis revealed that cobratoxin binding to this protein significantly dampened the axially symmetric motion of the AChBP that may be associated with channel gating in the full nAChR. The results suggest that alterations in receptor dynamics could be a general feature of ligand binding.

Place, publisher, year, edition, pages
2008. Vol. 48, no 4, 855-860 p.
National Category
Biophysics Theoretical Chemistry Bioinformatics and Systems Biology
Identifiers
URN: urn:nbn:se:kth:diva-82622DOI: 10.1021/ci700456sISI: 000255448400015PubMedID: 18348519OAI: oai:DiVA.org:kth-82622DiVA: diva2:498464
Note
QC 20120217Available from: 2012-02-12 Created: 2012-02-12 Last updated: 2012-02-17Bibliographically approved

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Lindahl, Erik

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