2qqh: Difference between revisions

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==Overview==

Membrane attack is important for mammalian immune defense against invading, microorganisms and infected host cells. Proteins of the complement, membrane attack complex (MAC) and the protein perforin share a common, MACPF domain that is responsible for membrane insertion and pore, formation. We determined the crystal structure of the MACPF domain of, complement component C8alpha at 2.5 angstrom resolution and show that it, is structurally homologous to the bacterial, pore-forming, cholesterol-dependent cytolysins. The structure displays two regions that, (in the bacterial cytolysins) refold into transmembrane beta hairpins, forming the lining of a barrel pore. Local hydrophobicity explains why, C8alpha is the first complement protein to insert into the membrane. The, size of the MACPF domain is consistent with known C9 pore sizes. These, data imply that these mammalian and bacterial cytolytic proteins share a, common mechanism of membrane insertion.

Membrane attack is important for mammalian immune defense against invading microorganisms and infected host cells. Proteins of the complement membrane attack complex (MAC) and the protein perforin share a common MACPF domain that is responsible for membrane insertion and pore formation. We determined the crystal structure of the MACPF domain of complement component C8alpha at 2.5 angstrom resolution and show that it is structurally homologous to the bacterial, pore-forming, cholesterol-dependent cytolysins. The structure displays two regions that (in the bacterial cytolysins) refold into transmembrane beta hairpins, forming the lining of a barrel pore. Local hydrophobicity explains why C8alpha is the first complement protein to insert into the membrane. The size of the MACPF domain is consistent with known C9 pore sizes. These data imply that these mammalian and bacterial cytolytic proteins share a common mechanism of membrane insertion.

==Disease==

Known disease associated with this structure: C8 deficiency, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120950 120950]]

==About this Structure==

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[[Category: Single protein]]

[[Category: Gros, P.]]

[[Category: Hadders, M.A.]]

[[Category: Hadders, M A.]]

[[Category: NI]]

[[Category: SO4]]

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[[Category: secreted]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:27 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Membrane attack is important for mammalian immune defense against invading, microorganisms and infected host cells. Proteins of the complement, membrane attack complex (MAC) and the protein perforin share a common, MACPF domain that is responsible for membrane insertion and pore, formation. We determined the crystal structure of the MACPF domain of, complement component C8alpha at 2.5 angstrom resolution and show that it, is structurally homologous to the bacterial, pore-forming, cholesterol-dependent cytolysins. The structure displays two regions that, (in the bacterial cytolysins) refold into transmembrane beta hairpins, forming the lining of a barrel pore. Local hydrophobicity explains why, C8alpha is the first complement protein to insert into the membrane. The, size of the MACPF domain is consistent with known C9 pore sizes. These, data imply that these mammalian and bacterial cytolytic proteins share a, common mechanism of membrane insertion.
+Membrane attack is important for mammalian immune defense against invading microorganisms and infected host cells. Proteins of the complement membrane attack complex (MAC) and the protein perforin share a common MACPF domain that is responsible for membrane insertion and pore formation. We determined the crystal structure of the MACPF domain of complement component C8alpha at 2.5 angstrom resolution and show that it is structurally homologous to the bacterial, pore-forming, cholesterol-dependent cytolysins. The structure displays two regions that (in the bacterial cytolysins) refold into transmembrane beta hairpins, forming the lining of a barrel pore. Local hydrophobicity explains why C8alpha is the first complement protein to insert into the membrane. The size of the MACPF domain is consistent with known C9 pore sizes. These data imply that these mammalian and bacterial cytolytic proteins share a common mechanism of membrane insertion.
+==Disease==
+Known disease associated with this structure: C8 deficiency, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120950 120950]]
 ==About this Structure==
@@ Line 14: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Gros, P.]]
-[[Category: Hadders, M.A.]]
+[[Category: Hadders, M A.]]
 [[Category: NI]]
 [[Category: SO4]]
@@ Line 33: / Line 36: @@
 [[Category: secreted]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:58:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:27 2008''