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. 1995 Jan;4(1):75–83. doi: 10.1002/pro.5560040110

A comparison of X-ray and NMR structures for human endothelin-1.

B A Wallace 1, R W Janes 1, D A Bassolino 1, S R Krystek Jr 1
PMCID: PMC2142965  PMID: 7773179

Abstract

Direct comparisons between the recently solved X-ray and NMR structures of human endothelin-1 with respect to secondary structure, RMS deviations, surface accessibilities, and side-chain conformers indicate important differences in conformation, especially in the C-terminus, but also in the central loop region, that are important for defining the specificity of binding. These differences are larger than seen for other X-ray and NMR structures that have been compared. Comparisons between the X-ray structure and the NMR NOE constraints highlight the regions of flexibility and environment-induced diversity in the endothelin structures.

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Selected References

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