1edn: Difference between revisions

Line 1:

[[Image:1edn.~~gif~~|left|200px]]

[[Image:1edn.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~HUMAN ENDOTHELIN-1~~'''~~

===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.

The line below this paragraph, {{ABSTRACT_PUBMED_7664037}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7664037 is the PubMed ID number.

-->

==About this Structure==

Line 25:

Line 29:

[[Category: Wallace, B A.]]

[[Category: Signal polypeptide g-protein coupled-receptor ligand]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 14~~:58:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:32:11 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1edn.gif|left|200px]]
+{{Seed}}
+[[Image:1edn.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1edn|  PDB=1edn  |  SCENE=  }}
-'''HUMAN ENDOTHELIN-1'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7664037}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7664037 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7664037}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Wallace, B A.]]
 [[Category: Signal polypeptide g-protein coupled-receptor ligand]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:58:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:32:11 2008''