1ok3: Difference between revisions

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[[Image:1ok3.~~gif~~|left|200px]]

[[Image:1ok3.png|left|200px]]

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~~'''~~DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.~~'''~~

===DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.===

~~==Overview==~~

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~~The human complement regulator CD55 is a key molecule protecting self~~-~~cells from complement~~-~~mediated lysis. X-ray diffraction and analytical ultracentrifugation data reveal a rod-like arrangement of four short consensus repeat (SCR) domains in both the crystal and solution.~~ The ~~stalk linking~~ the ~~four SCR domains~~ to the ~~glycosylphosphatidylinositol anchor is extended by the addition of 11 highly charged O-glycans and positions the domains an estimated 177 A above the membrane~~. ~~Mutation mapping and hydrophobic potential analysis suggest that the interaction with the convertase~~, ~~and thus complement regulation, depends on the burial of a hydrophobic patch centered on~~ the ~~linker between SCR domains 2 and 3~~.

The line below this paragraph, {{ABSTRACT_PUBMED_14734808}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 14734808 is the PubMed ID number.

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==About this Structure==

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[[Category: Regulator of complement]]

[[Category: Short consensus repeat domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 03~~:57:02 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:10:46 2008''

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-[[Image:1ok3.gif|left|200px]]
+{{Seed}}
+[[Image:1ok3.png|left|200px]]
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 {{STRUCTURE_1ok3|  PDB=1ok3  |  SCENE=  }}
-'''DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.'''
+===DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.===
-==Overview==
+<!--
-The human complement regulator CD55 is a key molecule protecting self-cells from complement-mediated lysis. X-ray diffraction and analytical ultracentrifugation data reveal a rod-like arrangement of four short consensus repeat (SCR) domains in both the crystal and solution. The stalk linking the four SCR domains to the glycosylphosphatidylinositol anchor is extended by the addition of 11 highly charged O-glycans and positions the domains an estimated 177 A above the membrane. Mutation mapping and hydrophobic potential analysis suggest that the interaction with the convertase, and thus complement regulation, depends on the burial of a hydrophobic patch centered on the linker between SCR domains 2 and 3.
+The line below this paragraph, {{ABSTRACT_PUBMED_14734808}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14734808 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14734808}}
 ==About this Structure==
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 [[Category: Regulator of complement]]
 [[Category: Short consensus repeat domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:57:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:10:46 2008''