1edn

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1edn, resolution 2.18Å

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HUMAN ENDOTHELIN-1

Overview

The three-dimensional structure of the vasoactive polypeptide endothelin, the most potent vasoconstrictor yet identified, has been determined by, X-ray crystallography to 2.18 A resolution. This intermediate-sized, structure was solved by molecular replacement techniques using a fragment, of an NMR-derived model for initial phasing of the data. However, comparisons of the final X-ray structure with the many diverse models, derived from NMR data indicate some important differences, especially in, the carboxy-terminal region of the molecule: the entire carboxy terminal, tail (residues 16-21) is helical in the crystal structure, but not in any, of the NMR structures. This may be a functionally significant difference, as this region is crucial for receptor binding and vasoactivity.

About this Structure

1EDN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of human endothelin., Janes RW, Peapus DH, Wallace BA, Nat Struct Biol. 1994 May;1(5):311-9. PMID:7664037

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