1cly: Difference between revisions

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

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

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

caption="1cly, resolution 2.5Å" />

'''IGG FAB (HUMAN IGG1, KAPPA) CHIMERIC FRAGMENT (CBR96) COMPLEXED WITH LEWIS Y NONOATE METHYL ESTER'''<br />

==Overview==

The crystal structures of the murine BR96 Fab and its human chimera have, been determined in complex with the nonoate methyl ester derivative of, Lewis Y (nLey) at 2.8 A and 2.5 A resolution, respectively. BR96 binds the, carbohydrate in a large pocket which is formed by residues of all CDR, loops except L2. The binding of the carbohydrate is mediated predominantly, by aromatic residues in BR96. Analysis of the structure suggests that BR96, is capable of recognizing a structure larger than the Le(y), tetrasaccharide, providing a possible explanation for its high tumour, selectivity. The structure provides a rationale for mutagenesis, experiments that have resulted in BR96 CDR loop mutants with increased, affinity for nLey and/or tumour cells.

The crystal structures of the murine BR96 Fab and its human chimera have been determined in complex with the nonoate methyl ester derivative of Lewis Y (nLey) at 2.8 A and 2.5 A resolution, respectively. BR96 binds the carbohydrate in a large pocket which is formed by residues of all CDR loops except L2. The binding of the carbohydrate is mediated predominantly by aromatic residues in BR96. Analysis of the structure suggests that BR96 is capable of recognizing a structure larger than the Le(y) tetrasaccharide, providing a possible explanation for its high tumour selectivity. The structure provides a rationale for mutagenesis experiments that have resulted in BR96 CDR loop mutants with increased affinity for nLey and/or tumour cells.

==About this Structure==

1CLY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NON as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CLY OCA].

1CLY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NON:'>NON</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLY OCA].

==Reference==

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[[Category: immunoglobulin c region]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 18 09~~:27:~~42 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:26 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1cly.gif|left|200px]]<br />
+[[Image:1cly.gif|left|200px]]<br /><applet load="1cly" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1cly" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1cly, resolution 2.5&Aring;" />
 '''IGG FAB (HUMAN IGG1, KAPPA) CHIMERIC FRAGMENT (CBR96) COMPLEXED WITH LEWIS Y NONOATE METHYL ESTER'''<br />
 ==Overview==
-The crystal structures of the murine BR96 Fab and its human chimera have, been determined in complex with the nonoate methyl ester derivative of, Lewis Y (nLey) at 2.8 A and 2.5 A resolution, respectively. BR96 binds the, carbohydrate in a large pocket which is formed by residues of all CDR, loops except L2. The binding of the carbohydrate is mediated predominantly, by aromatic residues in BR96. Analysis of the structure suggests that BR96, is capable of recognizing a structure larger than the Le(y), tetrasaccharide, providing a possible explanation for its high tumour, selectivity. The structure provides a rationale for mutagenesis, experiments that have resulted in BR96 CDR loop mutants with increased, affinity for nLey and/or tumour cells.
+The crystal structures of the murine BR96 Fab and its human chimera have been determined in complex with the nonoate methyl ester derivative of Lewis Y (nLey) at 2.8 A and 2.5 A resolution, respectively. BR96 binds the carbohydrate in a large pocket which is formed by residues of all CDR loops except L2. The binding of the carbohydrate is mediated predominantly by aromatic residues in BR96. Analysis of the structure suggests that BR96 is capable of recognizing a structure larger than the Le(y) tetrasaccharide, providing a possible explanation for its high tumour selectivity. The structure provides a rationale for mutagenesis experiments that have resulted in BR96 CDR loop mutants with increased affinity for nLey and/or tumour cells.
 ==About this Structure==
-CLY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NON as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CLY OCA].
+CLY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NON:'>NON</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLY OCA].
 ==Reference==
@@ Line 22: / Line 21: @@
 [[Category: immunoglobulin c region]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:27:42 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:26 2008''