1edn
From Proteopedia
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'''HUMAN ENDOTHELIN-1''' | '''HUMAN ENDOTHELIN-1''' | ||
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[[Category: Janes, R W.]] | [[Category: Janes, R W.]] | ||
[[Category: Wallace, B A.]] | [[Category: Wallace, B A.]] | ||
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Revision as of 11:58, 2 May 2008
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 Page seeded by OCA on Fri May 2 14:58:09 2008
