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==Overview==

Factor B is the central protease of the complement system of immune, defense. Here, we present the crystal structure of human factor B at 2.3-A, resolution, which reveals how the five-domain proenzyme is kept securely, inactive. The canonical activation helix of the Von Willebrand factor A, (VWA) domain is displaced by a helix from the preceding domain linker. The, two helices conformationally link the scissile-activation peptide and the, metal ion-dependent adhesion site required for binding of the ligand C3b., The data suggest that C3b binding displaces the three N-terminal control, domains and reshuffles the two central helices. Reshuffling of the helices, releases the scissile bond for final proteolytic activation and generates, a new interface between the VWA domain and the serine protease domain., This allosteric mechanism is crucial for tight regulation of the, complement-amplification step in the immune response.

Factor B is the central protease of the complement system of immune defense. Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive. The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker. The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b. The data suggest that C3b binding displaces the three N-terminal control domains and reshuffles the two central helices. Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain. This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.

==Disease==

Known diseases associated with this structure: Macular degeneration, age-related, reduced risk of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138470 138470]]

==About this Structure==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Daha, M.R.]]

[[Category: Daha, M R.]]

[[Category: Gomes, L.]]

[[Category: Gros, P.]]

[[Category: Hemrika, W.]]

[[Category: Huizinga, E.G.]]

[[Category: Huizinga, E G.]]

[[Category: Janssen, B.J.C.]]

[[Category: Janssen, B J.C.]]

[[Category: Milder, F.J.]]

[[Category: Milder, F J.]]

[[Category: Romijn, R.A.]]

[[Category: Romijn, R A.]]

[[Category: Roos, A.]]

[[Category: Schouten, A.]]

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[[Category: von willebrand factor-a domain]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:34 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Factor B is the central protease of the complement system of immune, defense. Here, we present the crystal structure of human factor B at 2.3-A, resolution, which reveals how the five-domain proenzyme is kept securely, inactive. The canonical activation helix of the Von Willebrand factor A, (VWA) domain is displaced by a helix from the preceding domain linker. The, two helices conformationally link the scissile-activation peptide and the, metal ion-dependent adhesion site required for binding of the ligand C3b., The data suggest that C3b binding displaces the three N-terminal control, domains and reshuffles the two central helices. Reshuffling of the helices, releases the scissile bond for final proteolytic activation and generates, a new interface between the VWA domain and the serine protease domain., This allosteric mechanism is crucial for tight regulation of the, complement-amplification step in the immune response.
+Factor B is the central protease of the complement system of immune defense. Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive. The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker. The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b. The data suggest that C3b binding displaces the three N-terminal control domains and reshuffles the two central helices. Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain. This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
+==Disease==
+Known diseases associated with this structure: Macular degeneration, age-related, reduced risk of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138470 138470]]
 ==About this Structure==
@@ Line 14: / Line 17: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Daha, M.R.]]
+[[Category: Daha, M R.]]
 [[Category: Gomes, L.]]
 [[Category: Gros, P.]]
 [[Category: Hemrika, W.]]
-[[Category: Huizinga, E.G.]]
+[[Category: Huizinga, E G.]]
-[[Category: Janssen, B.J.C.]]
+[[Category: Janssen, B J.C.]]
-[[Category: Milder, F.J.]]
+[[Category: Milder, F J.]]
-[[Category: Romijn, R.A.]]
+[[Category: Romijn, R A.]]
 [[Category: Roos, A.]]
 [[Category: Schouten, A.]]
@@ Line 31: / Line 34: @@
 [[Category: von willebrand factor-a domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:04:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:34 2008''