1edn
From Proteopedia
(Difference between revisions)
m (Protected "1edn" [edit=sysop:move=sysop]) |
|||
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1edn.png|left|200px]] | ||
| - | + | ==HUMAN ENDOTHELIN-1== | |
| + | <StructureSection load='1edn' size='340' side='right'caption='[[1edn]], [[Resolution|resolution]] 2.18Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1edn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1edn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edn OCA], [https://pdbe.org/1edn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edn RCSB], [https://www.ebi.ac.uk/pdbsum/1edn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/EDN1_HUMAN EDN1_HUMAN] Endothelins are endothelium-derived vasoconstrictor peptides. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | The crystal structure of human endothelin.,Janes RW, Peapus DH, Wallace BA Nat Struct Biol. 1994 May;1(5):311-9. PMID:7664037<ref>PMID:7664037</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | == | + | </div> |
| - | + | <div class="pdbe-citations 1edn" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Janes RW]] |
| - | [[Category: | + | [[Category: Wallace BA]] |
| - | + | ||
Current revision
HUMAN ENDOTHELIN-1
| |||||||||||
