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1sbs

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(New page: 200px<br /> <applet load="1sbs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sbs, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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<applet load="1sbs" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF AN ANTI-HCG FAB'''<br />
'''CRYSTAL STRUCTURE OF AN ANTI-HCG FAB'''<br />
==Overview==
==Overview==
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3A2 is an antibody raised against human chorionic gonadotropin and, recognizes a linear epitope on the C-terminal peptide of the human, chorionic gonadotropin beta-subunit. Its three-dimensional structure has, been determined to 2-A resolution using molecular replacement and refined, to a conventional R-factor of 18.2%. The protein exhibits the typical, immunoglobulin fold, and the model contains 944 ordered water molecules, and one sulfate ion. A comparison of the complementarity-determining, regions of the Fab3A2 with those from the Protein Data Bank following the, canonical structure method reveals a canonical main chain conformation., This antibody belongs to the canonical structure class (combination of, canonical conformations of the complementarity determining loops) that, shows a preference for haptens and not for peptides. However, the shape of, the surface of the antigen binding loops resembles that of an anti-peptide, antibody.
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3A2 is an antibody raised against human chorionic gonadotropin and recognizes a linear epitope on the C-terminal peptide of the human chorionic gonadotropin beta-subunit. Its three-dimensional structure has been determined to 2-A resolution using molecular replacement and refined to a conventional R-factor of 18.2%. The protein exhibits the typical immunoglobulin fold, and the model contains 944 ordered water molecules and one sulfate ion. A comparison of the complementarity-determining regions of the Fab3A2 with those from the Protein Data Bank following the canonical structure method reveals a canonical main chain conformation. This antibody belongs to the canonical structure class (combination of canonical conformations of the complementarity determining loops) that shows a preference for haptens and not for peptides. However, the shape of the surface of the antigen binding loops resembles that of an anti-peptide antibody.
==About this Structure==
==About this Structure==
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1SBS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SBS OCA].
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1SBS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBS OCA].
==Reference==
==Reference==
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[[Category: Emsley, P.]]
[[Category: Emsley, P.]]
[[Category: Fotinou, C.]]
[[Category: Fotinou, C.]]
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[[Category: Isaacs, N.W.]]
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[[Category: Isaacs, N W.]]
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[[Category: Schielen, W.J.G.]]
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[[Category: Schielen, W J.G.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: fab-fragment]]
[[Category: fab-fragment]]
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[[Category: reproduction]]
[[Category: reproduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:42:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:54 2008''

Revision as of 12:59, 21 February 2008


1sbs, resolution 2.0Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF AN ANTI-HCG FAB

Overview

3A2 is an antibody raised against human chorionic gonadotropin and recognizes a linear epitope on the C-terminal peptide of the human chorionic gonadotropin beta-subunit. Its three-dimensional structure has been determined to 2-A resolution using molecular replacement and refined to a conventional R-factor of 18.2%. The protein exhibits the typical immunoglobulin fold, and the model contains 944 ordered water molecules and one sulfate ion. A comparison of the complementarity-determining regions of the Fab3A2 with those from the Protein Data Bank following the canonical structure method reveals a canonical main chain conformation. This antibody belongs to the canonical structure class (combination of canonical conformations of the complementarity determining loops) that shows a preference for haptens and not for peptides. However, the shape of the surface of the antigen binding loops resembles that of an anti-peptide antibody.

About this Structure

1SBS is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of an Fab fragment against a C-terminal peptide of hCG at 2.0 A resolution., Fotinou C, Beauchamp J, Emsley P, deHaan A, Schielen WJ, Bos E, Isaacs NW, J Biol Chem. 1998 Aug 28;273(35):22515-8. PMID:9712877

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