2ihl
From Proteopedia
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|PDB= 2ihl |SIZE=350|CAPTION= <scene name='initialview01'>2ihl</scene>, resolution 1.4Å | |PDB= 2ihl |SIZE=350|CAPTION= <scene name='initialview01'>2ihl</scene>, resolution 1.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ihl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihl OCA], [http://www.ebi.ac.uk/pdbsum/2ihl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ihl RCSB]</span> | ||
}} | }} | ||
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[[Category: Souchon, H.]] | [[Category: Souchon, H.]] | ||
[[Category: Zhang, Z.]] | [[Category: Zhang, Z.]] | ||
| - | [[Category: NA]] | ||
[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:44:25 2008'' |
Revision as of 00:44, 31 March 2008
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| , resolution 1.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LYSOZYME (E.C.3.2.1.17) (JAPANESE QUAIL)
Overview
Although antibodies are highly specific, cross-reactions are frequently observed. To understand the molecular basis of this phenomenon, we studied the anti-hen egg lysozyme (HEL) monoclonal antibody (mAb) D11.15, which cross-reacts with several avian lysozymes, in some cases with a higher affinity (heteroclitic binding) than for HEL. We have determined the crystal structure of the Fv fragment of D11.15 complexed with pheasant egg lysozyme (PHL). In addition, we have determined the structure of PHL, Guinea fowl egg lysozyme, and Japanese quail egg lysozyme. Differences in the affinity of D11.15 for the lysozymes appear to result from sequence substitutions in these antigens at the interface with the antibody. More generally, cross-reactivity is seen to require a stereochemically permissive environment for the variant antigen residues at the antibody-antigen interface.
About this Structure
2IHL is a Single protein structure of sequence from Coturnix japonica. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex., Chitarra V, Alzari PM, Bentley GA, Bhat TN, Eisele JL, Houdusse A, Lescar J, Souchon H, Poljak RJ, Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7711-5. PMID:8356074
Page seeded by OCA on Mon Mar 31 03:44:25 2008
