1f90: Difference between revisions

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[[Image:1f90.gif|left|200px]]<br />

[[Image:1f90.gif|left|200px]]<br /><applet load="1f90" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1f90" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1f90, resolution 2.6Å" />

'''FAB FRAGMENT OF MONOCLONAL ANTIBODY (LNKB-2) AGAINST HUMAN INTERLEUKIN-2 IN COMPLEX WITH ANTIGENIC PEPTIDE'''<br />

==Overview==

The three-dimensional structure of the Fab fragment of a monoclonal, antibody (LNKB-2) to human interleukin-2 (IL-2) complexed with a synthetic, antigenic nonapeptide, Ac-Lys-Pro-Leu-Glu-Glu-Val-Leu-Asn-Leu-OMe, has, been determined at 3.0 A resolution. In the structure, four out of the six, hypervariable loops of the Fab (complementarity determining regions [CDRs], L1, H1, H2, and H3) are involved in peptide association through hydrogen, bonding, salt bridge formation, and hydrophobic interactions. The Tyr, residues in the Fab antigen binding site play a major role in, antigen-antibody recognition. The structures of the complexed and, uncomplexed Fab were compared. In the antigen binding site the CDR-L1 loop, of the antibody shows the largest structural changes upon peptide binding., The peptide adopts a mostly alpha-helical conformation similar to that in, the epitope fragment 64-72 of the IL-2 antigen. The side chains of, residues Leu 66, Val 69, and Leu 70, which are shielded internally in the, IL-2 structure, are involved in interactions with the Fab in the complex, studied. This indicates that antibody-antigen complexation involves a, significant rearrangement of the epitope-containing region of the IL-2, with retention of the alpha-helical character of the epitope fragment.

The three-dimensional structure of the Fab fragment of a monoclonal antibody (LNKB-2) to human interleukin-2 (IL-2) complexed with a synthetic antigenic nonapeptide, Ac-Lys-Pro-Leu-Glu-Glu-Val-Leu-Asn-Leu-OMe, has been determined at 3.0 A resolution. In the structure, four out of the six hypervariable loops of the Fab (complementarity determining regions [CDRs] L1, H1, H2, and H3) are involved in peptide association through hydrogen bonding, salt bridge formation, and hydrophobic interactions. The Tyr residues in the Fab antigen binding site play a major role in antigen-antibody recognition. The structures of the complexed and uncomplexed Fab were compared. In the antigen binding site the CDR-L1 loop of the antibody shows the largest structural changes upon peptide binding. The peptide adopts a mostly alpha-helical conformation similar to that in the epitope fragment 64-72 of the IL-2 antigen. The side chains of residues Leu 66, Val 69, and Leu 70, which are shielded internally in the IL-2 structure, are involved in interactions with the Fab in the complex studied. This indicates that antibody-antigen complexation involves a significant rearrangement of the epitope-containing region of the IL-2 with retention of the alpha-helical character of the epitope fragment.

==About this Structure==

1F90 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1F90 OCA].

1F90 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F90 OCA].

==Reference==

Line 14:

Line 13:

[[Category: Mus musculus]]

[[Category: Protein complex]]

[[Category: Afonin, P.V.]]

[[Category: Afonin, P V.]]

[[Category: Duax, W.L.]]

[[Category: Duax, W L.]]

[[Category: Fokin, A.V.]]

[[Category: Fokin, A V.]]

[[Category: Ivanov, V.T.]]

[[Category: Ivanov, V T.]]

[[Category: Li, N.]]

[[Category: Mareeva, T.Y.]]

[[Category: Mareeva, T Y.]]

[[Category: Mikhailova, I.Y.]]

[[Category: Mikhailova, I Y.]]

[[Category: Mikhaleva, I.I.]]

[[Category: Mikhaleva, I I.]]

[[Category: Nesmeyanov, V.A.]]

[[Category: Nesmeyanov, V A.]]

[[Category: Onoprienko, L.V.]]

[[Category: Onoprienko, L V.]]

[[Category: Pletnev, V.Z.]]

[[Category: Pletnev, V Z.]]

[[Category: Tsigannik, I.N.]]

[[Category: Tsigannik, I N.]]

[[Category: antigen-binding fragment]]

[[Category: antigenic peptide]]

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Line 30:

[[Category: monoclonal antibody]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 18 09~~:29:~~56 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:14 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1f90.gif|left|200px]]<br />
+[[Image:1f90.gif|left|200px]]<br /><applet load="1f90" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1f90" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1f90, resolution 2.6&Aring;" />
 '''FAB FRAGMENT OF MONOCLONAL ANTIBODY (LNKB-2) AGAINST HUMAN INTERLEUKIN-2 IN COMPLEX WITH ANTIGENIC PEPTIDE'''<br />
 ==Overview==
-The three-dimensional structure of the Fab fragment of a monoclonal, antibody (LNKB-2) to human interleukin-2 (IL-2) complexed with a synthetic, antigenic nonapeptide, Ac-Lys-Pro-Leu-Glu-Glu-Val-Leu-Asn-Leu-OMe, has, been determined at 3.0 A resolution. In the structure, four out of the six, hypervariable loops of the Fab (complementarity determining regions [CDRs], L1, H1, H2, and H3) are involved in peptide association through hydrogen, bonding, salt bridge formation, and hydrophobic interactions. The Tyr, residues in the Fab antigen binding site play a major role in, antigen-antibody recognition. The structures of the complexed and, uncomplexed Fab were compared. In the antigen binding site the CDR-L1 loop, of the antibody shows the largest structural changes upon peptide binding., The peptide adopts a mostly alpha-helical conformation similar to that in, the epitope fragment 64-72 of the IL-2 antigen. The side chains of, residues Leu 66, Val 69, and Leu 70, which are shielded internally in the, IL-2 structure, are involved in interactions with the Fab in the complex, studied. This indicates that antibody-antigen complexation involves a, significant rearrangement of the epitope-containing region of the IL-2, with retention of the alpha-helical character of the epitope fragment.
+The three-dimensional structure of the Fab fragment of a monoclonal antibody (LNKB-2) to human interleukin-2 (IL-2) complexed with a synthetic antigenic nonapeptide, Ac-Lys-Pro-Leu-Glu-Glu-Val-Leu-Asn-Leu-OMe, has been determined at 3.0 A resolution. In the structure, four out of the six hypervariable loops of the Fab (complementarity determining regions [CDRs] L1, H1, H2, and H3) are involved in peptide association through hydrogen bonding, salt bridge formation, and hydrophobic interactions. The Tyr residues in the Fab antigen binding site play a major role in antigen-antibody recognition. The structures of the complexed and uncomplexed Fab were compared. In the antigen binding site the CDR-L1 loop of the antibody shows the largest structural changes upon peptide binding. The peptide adopts a mostly alpha-helical conformation similar to that in the epitope fragment 64-72 of the IL-2 antigen. The side chains of residues Leu 66, Val 69, and Leu 70, which are shielded internally in the IL-2 structure, are involved in interactions with the Fab in the complex studied. This indicates that antibody-antigen complexation involves a significant rearrangement of the epitope-containing region of the IL-2 with retention of the alpha-helical character of the epitope fragment.
 ==About this Structure==
-F90 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F90 OCA].
+F90 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F90 OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Afonin, P.V.]]
+[[Category: Afonin, P V.]]
-[[Category: Duax, W.L.]]
+[[Category: Duax, W L.]]
-[[Category: Fokin, A.V.]]
+[[Category: Fokin, A V.]]
-[[Category: Ivanov, V.T.]]
+[[Category: Ivanov, V T.]]
 [[Category: Li, N.]]
-[[Category: Mareeva, T.Y.]]
+[[Category: Mareeva, T Y.]]
-[[Category: Mikhailova, I.Y.]]
+[[Category: Mikhailova, I Y.]]
-[[Category: Mikhaleva, I.I.]]
+[[Category: Mikhaleva, I I.]]
-[[Category: Nesmeyanov, V.A.]]
+[[Category: Nesmeyanov, V A.]]
-[[Category: Onoprienko, L.V.]]
+[[Category: Onoprienko, L V.]]
-[[Category: Pletnev, V.Z.]]
+[[Category: Pletnev, V Z.]]
-[[Category: Tsigannik, I.N.]]
+[[Category: Tsigannik, I N.]]
 [[Category: antigen-binding fragment]]
 [[Category: antigenic peptide]]
@@ Line 31: / Line 30: @@
 [[Category: monoclonal antibody]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:29:56 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:14 2008''