2d03: Difference between revisions

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[[Image:2d03.gif|left|200px]]<br />

[[Image:2d03.gif|left|200px]]<br /><applet load="2d03" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2d03" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2d03, resolution 1.97Å" />

'''Crystal structure of the G91S mutant of the NNA7 Fab'''<br />

==Overview==

The NNA7 Fab antibody fragment recognizes the human N-type blood-group, antigen comprised of the N-terminal glycopeptide of glycophorin A (GPA). A, mutant form of this Fab fragment, NNA7-G91S, exhibits markedly reduced, antigen binding. To provide insight into how these Fab fragments recognize, this glycopeptide antigen, the crystal structures of NNA7 and NNA7-G91S, were solved and refined to 1.83 and 1.97 A resolution, respectively. Both, molecules are composed of the same heavy (H) chain Fd fragment, but each, contains a slightly different light (L) chain owing to the G91S, substitution. Specifically, the G91S mutation pushes the backbone of the, neighboring H chain away from complementarity-determining region 3 (CDR3), of the L-chain variable region, allowing an additional glycerol, cryoprotectant molecule to enter the antigen-combining site near the, putative location of O-linked glycosylation. Each Fab fragment also, possesses a well defined 2-(N-morpholino)ethanesulfonic acid (MES), molecule trapped in its antigen-combining site, as well as a, crystallographic symmetry-related molecule comprising an amino-acid, sequence that is virtually identical to the N-terminus of GPA. The MES, molecule interacts with the H-chain CDR in a manner reminiscent of, antibody-carbohydrate complexes. These results suggest a model for, recognition of the glycopeptide antigen that accounts for the deleterious, effect of the G91S substitution.

The NNA7 Fab antibody fragment recognizes the human N-type blood-group antigen comprised of the N-terminal glycopeptide of glycophorin A (GPA). A mutant form of this Fab fragment, NNA7-G91S, exhibits markedly reduced antigen binding. To provide insight into how these Fab fragments recognize this glycopeptide antigen, the crystal structures of NNA7 and NNA7-G91S were solved and refined to 1.83 and 1.97 A resolution, respectively. Both molecules are composed of the same heavy (H) chain Fd fragment, but each contains a slightly different light (L) chain owing to the G91S substitution. Specifically, the G91S mutation pushes the backbone of the neighboring H chain away from complementarity-determining region 3 (CDR3) of the L-chain variable region, allowing an additional glycerol cryoprotectant molecule to enter the antigen-combining site near the putative location of O-linked glycosylation. Each Fab fragment also possesses a well defined 2-(N-morpholino)ethanesulfonic acid (MES) molecule trapped in its antigen-combining site, as well as a crystallographic symmetry-related molecule comprising an amino-acid sequence that is virtually identical to the N-terminus of GPA. The MES molecule interacts with the H-chain CDR in a manner reminiscent of antibody-carbohydrate complexes. These results suggest a model for recognition of the glycopeptide antigen that accounts for the deleterious effect of the G91S substitution.

==About this Structure==

2D03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MES, GOL and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2D03 OCA].

2D03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MES:'>MES</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D03 OCA].

==Reference==

Line 14:

Line 13:

[[Category: Mus musculus]]

[[Category: Single protein]]

[[Category: Song, S.C.]]

[[Category: Song, S C.]]

[[Category: Spitalnik, S.L.]]

[[Category: Spitalnik, S L.]]

[[Category: Wedekind, J.E.]]

[[Category: Wedekind, J E.]]

[[Category: Xie, K.]]

[[Category: GOL]]

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[[Category: antibody]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 18 09~~:48:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:03 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2d03.gif|left|200px]]<br />
+[[Image:2d03.gif|left|200px]]<br /><applet load="2d03" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2d03" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2d03, resolution 1.97&Aring;" />
 '''Crystal structure of the G91S mutant of the NNA7 Fab'''<br />
 ==Overview==
-The NNA7 Fab antibody fragment recognizes the human N-type blood-group, antigen comprised of the N-terminal glycopeptide of glycophorin A (GPA). A, mutant form of this Fab fragment, NNA7-G91S, exhibits markedly reduced, antigen binding. To provide insight into how these Fab fragments recognize, this glycopeptide antigen, the crystal structures of NNA7 and NNA7-G91S, were solved and refined to 1.83 and 1.97 A resolution, respectively. Both, molecules are composed of the same heavy (H) chain Fd fragment, but each, contains a slightly different light (L) chain owing to the G91S, substitution. Specifically, the G91S mutation pushes the backbone of the, neighboring H chain away from complementarity-determining region 3 (CDR3), of the L-chain variable region, allowing an additional glycerol, cryoprotectant molecule to enter the antigen-combining site near the, putative location of O-linked glycosylation. Each Fab fragment also, possesses a well defined 2-(N-morpholino)ethanesulfonic acid (MES), molecule trapped in its antigen-combining site, as well as a, crystallographic symmetry-related molecule comprising an amino-acid, sequence that is virtually identical to the N-terminus of GPA. The MES, molecule interacts with the H-chain CDR in a manner reminiscent of, antibody-carbohydrate complexes. These results suggest a model for, recognition of the glycopeptide antigen that accounts for the deleterious, effect of the G91S substitution.
+The NNA7 Fab antibody fragment recognizes the human N-type blood-group antigen comprised of the N-terminal glycopeptide of glycophorin A (GPA). A mutant form of this Fab fragment, NNA7-G91S, exhibits markedly reduced antigen binding. To provide insight into how these Fab fragments recognize this glycopeptide antigen, the crystal structures of NNA7 and NNA7-G91S were solved and refined to 1.83 and 1.97 A resolution, respectively. Both molecules are composed of the same heavy (H) chain Fd fragment, but each contains a slightly different light (L) chain owing to the G91S substitution. Specifically, the G91S mutation pushes the backbone of the neighboring H chain away from complementarity-determining region 3 (CDR3) of the L-chain variable region, allowing an additional glycerol cryoprotectant molecule to enter the antigen-combining site near the putative location of O-linked glycosylation. Each Fab fragment also possesses a well defined 2-(N-morpholino)ethanesulfonic acid (MES) molecule trapped in its antigen-combining site, as well as a crystallographic symmetry-related molecule comprising an amino-acid sequence that is virtually identical to the N-terminus of GPA. The MES molecule interacts with the H-chain CDR in a manner reminiscent of antibody-carbohydrate complexes. These results suggest a model for recognition of the glycopeptide antigen that accounts for the deleterious effect of the G91S substitution.
 ==About this Structure==
-D03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MES, GOL and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D03 OCA].
+D03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MES:'>MES</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D03 OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Song, S.C.]]
+[[Category: Song, S C.]]
-[[Category: Spitalnik, S.L.]]
+[[Category: Spitalnik, S L.]]
-[[Category: Wedekind, J.E.]]
+[[Category: Wedekind, J E.]]
 [[Category: Xie, K.]]
 [[Category: GOL]]
@@ Line 23: / Line 22: @@
 [[Category: antibody]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:48:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:03 2008''