2as8: Difference between revisions

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[[Image:2as8.gif|left|200px]]<br /><applet load="2as8" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2as8.gif|left|200px]]<br /><applet load="2as8" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2as8, resolution 1.950Å" />

'''Crystal structure of mature and fully active Der p 1 allergen'''<br />

==Overview==

BACKGROUND: Der p 1 is a 25-kd allergen with cysteine protease activity., Sensitization to Der p 1 affects a large proportion of individuals with, allergy, resulting in rhinitis, asthma, and/or atopic dermatitis., OBJECTIVE: We determined the Der p 1 crystallographic structure to, understand the relationships among structure, function, and allergenicity., METHODS: Recombinant pro-Der p 1 was produced in Pichia pastoris and, allowed to mature spontaneously before purification by a 2-step procedure., Protease activity was checked by using a fluorogenic peptide substrate., Allergenicity was analysed by IgE binding assays and basophil activation, test. The determination of the 3-dimensional structure was obtained by, X-ray crystallography at 1.9 A resolution. RESULTS: The recombinant, protein is fully active and expresses an allergenicity equivalent to its, natural counterpart. Der p 1 exhibits a cysteine protease fold typical of, the papain family, has a magnesium binding site, and forms dimers with a, large interface. The crystal lattice shows that the dimers are tightly, packed in a compact double layer of proteins. Such an assembly likely, exists in dry fecal pellets, the natural form of allergen exposure, and, appears ideal to interact with cell surface and trigger allergic, inflammation. CONCLUSION: We present here the 3-dimensional structural, features of mature fully active Der p 1, one of the main allergens, involved in human allergic diseases. This opens the possibility to, evaluate the importance of enzymatic activity in pathology and possible, new therapeutic interventions.

BACKGROUND: Der p 1 is a 25-kd allergen with cysteine protease activity. Sensitization to Der p 1 affects a large proportion of individuals with allergy, resulting in rhinitis, asthma, and/or atopic dermatitis. OBJECTIVE: We determined the Der p 1 crystallographic structure to understand the relationships among structure, function, and allergenicity. METHODS: Recombinant pro-Der p 1 was produced in Pichia pastoris and allowed to mature spontaneously before purification by a 2-step procedure. Protease activity was checked by using a fluorogenic peptide substrate. Allergenicity was analysed by IgE binding assays and basophil activation test. The determination of the 3-dimensional structure was obtained by X-ray crystallography at 1.9 A resolution. RESULTS: The recombinant protein is fully active and expresses an allergenicity equivalent to its natural counterpart. Der p 1 exhibits a cysteine protease fold typical of the papain family, has a magnesium binding site, and forms dimers with a large interface. The crystal lattice shows that the dimers are tightly packed in a compact double layer of proteins. Such an assembly likely exists in dry fecal pellets, the natural form of allergen exposure, and appears ideal to interact with cell surface and trigger allergic inflammation. CONCLUSION: We present here the 3-dimensional structural features of mature fully active Der p 1, one of the main allergens involved in human allergic diseases. This opens the possibility to evaluate the importance of enzymatic activity in pathology and possible new therapeutic interventions.

==About this Structure==

2AS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2AS8 OCA].

2AS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AS8 OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Carlier, V.]]

[[Category: Halleux, S.de.]]

[[Category: Halleux, S de.]]

[[Category: Jacquemin, M.]]

[[Category: Saint-Remy, J.M.]]

[[Category: Saint-Remy, J M.]]

[[Category: Stura, E.]]

[[Category: VanderElst, L.]]

Line 22:

[[Category: cysteine proteinase fold]]

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@@ Line 1: / Line 1: @@
-[[Image:2as8.gif|left|200px]]<br /><applet load="2as8" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2as8.gif|left|200px]]<br /><applet load="2as8" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2as8, resolution 1.950&Aring;" />
 '''Crystal structure of mature and fully active Der p 1 allergen'''<br />
 ==Overview==
-BACKGROUND: Der p 1 is a 25-kd allergen with cysteine protease activity., Sensitization to Der p 1 affects a large proportion of individuals with, allergy, resulting in rhinitis, asthma, and/or atopic dermatitis., OBJECTIVE: We determined the Der p 1 crystallographic structure to, understand the relationships among structure, function, and allergenicity., METHODS: Recombinant pro-Der p 1 was produced in Pichia pastoris and, allowed to mature spontaneously before purification by a 2-step procedure., Protease activity was checked by using a fluorogenic peptide substrate., Allergenicity was analysed by IgE binding assays and basophil activation, test. The determination of the 3-dimensional structure was obtained by, X-ray crystallography at 1.9 A resolution. RESULTS: The recombinant, protein is fully active and expresses an allergenicity equivalent to its, natural counterpart. Der p 1 exhibits a cysteine protease fold typical of, the papain family, has a magnesium binding site, and forms dimers with a, large interface. The crystal lattice shows that the dimers are tightly, packed in a compact double layer of proteins. Such an assembly likely, exists in dry fecal pellets, the natural form of allergen exposure, and, appears ideal to interact with cell surface and trigger allergic, inflammation. CONCLUSION: We present here the 3-dimensional structural, features of mature fully active Der p 1, one of the main allergens, involved in human allergic diseases. This opens the possibility to, evaluate the importance of enzymatic activity in pathology and possible, new therapeutic interventions.
+BACKGROUND: Der p 1 is a 25-kd allergen with cysteine protease activity. Sensitization to Der p 1 affects a large proportion of individuals with allergy, resulting in rhinitis, asthma, and/or atopic dermatitis. OBJECTIVE: We determined the Der p 1 crystallographic structure to understand the relationships among structure, function, and allergenicity. METHODS: Recombinant pro-Der p 1 was produced in Pichia pastoris and allowed to mature spontaneously before purification by a 2-step procedure. Protease activity was checked by using a fluorogenic peptide substrate. Allergenicity was analysed by IgE binding assays and basophil activation test. The determination of the 3-dimensional structure was obtained by X-ray crystallography at 1.9 A resolution. RESULTS: The recombinant protein is fully active and expresses an allergenicity equivalent to its natural counterpart. Der p 1 exhibits a cysteine protease fold typical of the papain family, has a magnesium binding site, and forms dimers with a large interface. The crystal lattice shows that the dimers are tightly packed in a compact double layer of proteins. Such an assembly likely exists in dry fecal pellets, the natural form of allergen exposure, and appears ideal to interact with cell surface and trigger allergic inflammation. CONCLUSION: We present here the 3-dimensional structural features of mature fully active Der p 1, one of the main allergens involved in human allergic diseases. This opens the possibility to evaluate the importance of enzymatic activity in pathology and possible new therapeutic interventions.
 ==About this Structure==
-AS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AS8 OCA].
+AS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AS8 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Carlier, V.]]
-[[Category: Halleux, S.de.]]
+[[Category: Halleux, S de.]]
 [[Category: Jacquemin, M.]]
-[[Category: Saint-Remy, J.M.]]
+[[Category: Saint-Remy, J M.]]
 [[Category: Stura, E.]]
 [[Category: VanderElst, L.]]
@@ Line 22: / Line 22: @@
 [[Category: cysteine proteinase fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:19:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:27 2008''