2g7i
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2g7i.gif|left|200px]] | [[Image:2g7i.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2g7i", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2g7i| PDB=2g7i | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''Structure of Human Complement Factor H Carboxyl Terminal Domains 19-20: a Basis for Atypical Hemolytic Uremic Syndrome''' | '''Structure of Human Complement Factor H Carboxyl Terminal Domains 19-20: a Basis for Atypical Hemolytic Uremic Syndrome''' | ||
| Line 28: | Line 25: | ||
[[Category: Jaakola, V P.]] | [[Category: Jaakola, V P.]] | ||
[[Category: Jokiranta, T S.]] | [[Category: Jokiranta, T S.]] | ||
| - | [[Category: | + | [[Category: Atypical hemolytic uremic syndrome]] |
| - | [[Category: | + | [[Category: Beta-1h globulin]] |
| - | [[Category: | + | [[Category: Complement]] |
| - | [[Category: | + | [[Category: Factor h]] |
| - | [[Category: | + | [[Category: Heparin binding]] |
| - | [[Category: | + | [[Category: Immune system]] |
| - | [[Category: | + | [[Category: Regulator]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:46:50 2008'' | |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:46, 4 May 2008
Structure of Human Complement Factor H Carboxyl Terminal Domains 19-20: a Basis for Atypical Hemolytic Uremic Syndrome
Overview
Factor H (FH) is the key regulator of the alternative pathway of complement. The carboxyl-terminal domains 19-20 of FH interact with the major opsonin C3b, glycosaminoglycans, and endothelial cells. Mutations within this area are associated with atypical haemolytic uremic syndrome (aHUS), a disease characterized by damage to endothelial cells, erythrocytes, and kidney glomeruli. The structure of recombinant FH19-20, solved at 1.8 A by X-ray crystallography, reveals that the short consensus repeat domain 20 contains, unusually, a short alpha-helix, and a patch of basic residues at its base. Most aHUS-associated mutations either destabilize the structure or cluster in a unique region on the surface of FH20. This region is close to, but distinct from, the primary heparin-binding patch of basic residues. By mutating five residues in this region, we show that it is involved, not in heparin, but in C3b binding. Therefore, the majority of the aHUS-associated mutations on the surface of FH19-20 interfere with the interaction between FH and C3b. This obviously leads to impaired control of complement attack on plasma-exposed cell surfaces in aHUS.
About this Structure
2G7I is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome., Jokiranta TS, Jaakola VP, Lehtinen MJ, Parepalo M, Meri S, Goldman A, EMBO J. 2006 Apr 19;25(8):1784-94. Epub 2006 Apr 6. PMID:16601698 Page seeded by OCA on Sun May 4 04:46:50 2008
