2jon: Difference between revisions

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==Overview==

Ole e 9 is an olive pollen allergen belonging to group 2 of, pathogenesis-related proteins. The protein is composed of two, immunological independent domains: an N-terminal domain (NtD) with, 1,3-beta-glucanase activity, and a C-terminal domain (CtD) that binds, 1,3-beta-glucans. We have determined the three-dimensional structure of, CtD-Ole e 9 (101 amino acids), which consists of two parallel, alpha-helices forming an angle of approximately 55 degrees , a small, antiparallel beta-sheet with two short strands, and a 3-10 helix turn, all, connected by long coil segments, resembling a novel type of folding among, allergens. Two regions surrounded by aromatic residues (F49, Y60, F96, Y91, and Y31, H68, Y65, F78) have been localized on the protein surface, and a, role for sugar binding is suggested. The epitope mapping of CtD-Ole e 9, shows that B-cell epitopes are mainly located on loops, although some of, them are contained in secondary structural elements. Interestingly, the, IgG and IgE epitopes are contiguous or overlapped, rather than coincident., The three-dimensional structure of CtD-Ole e 9 might help to understand, the underlying mechanism of its biochemical function and to determine, possible structure-allergenicity relationships.

Ole e 9 is an olive pollen allergen belonging to group 2 of pathogenesis-related proteins. The protein is composed of two immunological independent domains: an N-terminal domain (NtD) with 1,3-beta-glucanase activity, and a C-terminal domain (CtD) that binds 1,3-beta-glucans. We have determined the three-dimensional structure of CtD-Ole e 9 (101 amino acids), which consists of two parallel alpha-helices forming an angle of approximately 55 degrees , a small antiparallel beta-sheet with two short strands, and a 3-10 helix turn, all connected by long coil segments, resembling a novel type of folding among allergens. Two regions surrounded by aromatic residues (F49, Y60, F96, Y91 and Y31, H68, Y65, F78) have been localized on the protein surface, and a role for sugar binding is suggested. The epitope mapping of CtD-Ole e 9 shows that B-cell epitopes are mainly located on loops, although some of them are contained in secondary structural elements. Interestingly, the IgG and IgE epitopes are contiguous or overlapped, rather than coincident. The three-dimensional structure of CtD-Ole e 9 might help to understand the underlying mechanism of its biochemical function and to determine possible structure-allergenicity relationships.

==About this Structure==

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[[Category: Rodriguez, R.]]

[[Category: Santoro, J.]]

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

[[Category: Trevino, M A.]]

[[Category: Villalba, M.]]

[[Category: allergen]]

[[Category: olive pollen]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Ole e 9 is an olive pollen allergen belonging to group 2 of, pathogenesis-related proteins. The protein is composed of two, immunological independent domains: an N-terminal domain (NtD) with, 1,3-beta-glucanase activity, and a C-terminal domain (CtD) that binds, 1,3-beta-glucans. We have determined the three-dimensional structure of, CtD-Ole e 9 (101 amino acids), which consists of two parallel, alpha-helices forming an angle of approximately 55 degrees , a small, antiparallel beta-sheet with two short strands, and a 3-10 helix turn, all, connected by long coil segments, resembling a novel type of folding among, allergens. Two regions surrounded by aromatic residues (F49, Y60, F96, Y91, and Y31, H68, Y65, F78) have been localized on the protein surface, and a, role for sugar binding is suggested. The epitope mapping of CtD-Ole e 9, shows that B-cell epitopes are mainly located on loops, although some of, them are contained in secondary structural elements. Interestingly, the, IgG and IgE epitopes are contiguous or overlapped, rather than coincident., The three-dimensional structure of CtD-Ole e 9 might help to understand, the underlying mechanism of its biochemical function and to determine, possible structure-allergenicity relationships.
+Ole e 9 is an olive pollen allergen belonging to group 2 of pathogenesis-related proteins. The protein is composed of two immunological independent domains: an N-terminal domain (NtD) with 1,3-beta-glucanase activity, and a C-terminal domain (CtD) that binds 1,3-beta-glucans. We have determined the three-dimensional structure of CtD-Ole e 9 (101 amino acids), which consists of two parallel alpha-helices forming an angle of approximately 55 degrees , a small antiparallel beta-sheet with two short strands, and a 3-10 helix turn, all connected by long coil segments, resembling a novel type of folding among allergens. Two regions surrounded by aromatic residues (F49, Y60, F96, Y91 and Y31, H68, Y65, F78) have been localized on the protein surface, and a role for sugar binding is suggested. The epitope mapping of CtD-Ole e 9 shows that B-cell epitopes are mainly located on loops, although some of them are contained in secondary structural elements. Interestingly, the IgG and IgE epitopes are contiguous or overlapped, rather than coincident. The three-dimensional structure of CtD-Ole e 9 might help to understand the underlying mechanism of its biochemical function and to determine possible structure-allergenicity relationships.
 ==About this Structure==
@@ Line 19: / Line 19: @@
 [[Category: Rodriguez, R.]]
 [[Category: Santoro, J.]]
-[[Category: Trevino, M.A.]]
+[[Category: Trevino, M A.]]
 [[Category: Villalba, M.]]
 [[Category: allergen]]
 [[Category: olive pollen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:57:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:43 2008''