1ghf: Difference between revisions

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

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

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

caption="1ghf, resolution 2.7Å" />

'''ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT'''<br />

==Overview==

The structure of the Fab fragment of the mouse anti-anti-idiotypic, monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb, GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which, mimics the determinant defined by anti-human high molecular, weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments, of mAb GH1002 exist in the crystal as dimers related by crystallographic, 2-fold axes. The interface between dyad-related Fab fragments is formed, primarily by interaction of the hypervariable loops of one with the other., The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002, through their combining sites is extremely tight and intricate, closely, resembling that observed in structures of id-anti-id complexes, and, comparable in terms of total contact area, charge complementarity, and, number of hydrogen bonds. The self-complementarity of the antibody, observed here could be coincidental and thus reflect some non-specific, binding capability. It might, on the other hand, be immunologically, relevant and exemplify a certain degree of evolved self complementarity, characteristic of antibodies participating in idiotypic cascades.

The structure of the Fab fragment of the mouse anti-anti-idiotypic monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which mimics the determinant defined by anti-human high molecular weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments of mAb GH1002 exist in the crystal as dimers related by crystallographic 2-fold axes. The interface between dyad-related Fab fragments is formed primarily by interaction of the hypervariable loops of one with the other. The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002 through their combining sites is extremely tight and intricate, closely resembling that observed in structures of id-anti-id complexes, and comparable in terms of total contact area, charge complementarity, and number of hydrogen bonds. The self-complementarity of the antibody observed here could be coincidental and thus reflect some non-specific binding capability. It might, on the other hand, be immunologically relevant and exemplify a certain degree of evolved self complementarity characteristic of antibodies participating in idiotypic cascades.

==About this Structure==

1GHF 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=1GHF OCA].

1GHF 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=1GHF OCA].

==Reference==

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[[Category: antibody fab fragment]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 18 09~~:31:~~12 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:04 2008''

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-[[Image:1ghf.gif|left|200px]]<br />
+[[Image:1ghf.gif|left|200px]]<br /><applet load="1ghf" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1ghf" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ghf, resolution 2.7&Aring;" />
 '''ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT'''<br />
 ==Overview==
-The structure of the Fab fragment of the mouse anti-anti-idiotypic, monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb, GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which, mimics the determinant defined by anti-human high molecular, weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments, of mAb GH1002 exist in the crystal as dimers related by crystallographic, 2-fold axes. The interface between dyad-related Fab fragments is formed, primarily by interaction of the hypervariable loops of one with the other., The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002, through their combining sites is extremely tight and intricate, closely, resembling that observed in structures of id-anti-id complexes, and, comparable in terms of total contact area, charge complementarity, and, number of hydrogen bonds. The self-complementarity of the antibody, observed here could be coincidental and thus reflect some non-specific, binding capability. It might, on the other hand, be immunologically, relevant and exemplify a certain degree of evolved self complementarity, characteristic of antibodies participating in idiotypic cascades.
+The structure of the Fab fragment of the mouse anti-anti-idiotypic monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which mimics the determinant defined by anti-human high molecular weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments of mAb GH1002 exist in the crystal as dimers related by crystallographic 2-fold axes. The interface between dyad-related Fab fragments is formed primarily by interaction of the hypervariable loops of one with the other. The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002 through their combining sites is extremely tight and intricate, closely resembling that observed in structures of id-anti-id complexes, and comparable in terms of total contact area, charge complementarity, and number of hydrogen bonds. The self-complementarity of the antibody observed here could be coincidental and thus reflect some non-specific binding capability. It might, on the other hand, be immunologically relevant and exemplify a certain degree of evolved self complementarity characteristic of antibodies participating in idiotypic cascades.
 ==About this Structure==
-GHF 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=1GHF OCA].
+GHF 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=1GHF OCA].
 ==Reference==
@@ Line 21: / Line 20: @@
 [[Category: antibody fab fragment]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:31:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:04 2008''