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1j1x

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|SITE=
|SITE=
|LIGAND=
|LIGAND=
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|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]
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|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=
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|DOMAIN=
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|RELATEDENTRY=[[1c08|1C08]], [[1j1o|1J1O]], [[1j1p|1J1P]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j1x OCA], [http://www.ebi.ac.uk/pdbsum/1j1x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j1x RCSB]</span>
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[[Category: antigen-antibody complex]]
[[Category: antigen-antibody complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:57:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:27:44 2008''

Revision as of 18:27, 30 March 2008


PDB ID 1j1x

Drag the structure with the mouse to rotate
, resolution 1.8Å
Activity: Lysozyme, with EC number 3.2.1.17
Related: 1C08, 1J1O, 1J1P


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme


Overview

To study the role of hydrogen bonding via interfacial water molecules in protein-protein interactions, we examined the interaction between hen egg white lysozyme (HEL) and its HyHEL-10 variable domain fragment (Fv) antibody. We constructed three antibody mutants (l-Y50F, l-S91A, and l-S93A) and investigated the interactions between the mutant Fvs and HEL. Isothermal titration calorimetry indicated that the mutations significantly decreased the negative enthalpy change (8-25 kJ mol(-1)), despite some offset by a favorable entropy change. X-ray crystallography demonstrated that the complexes had nearly identical structures, including the positions of the interfacial water molecules. Taken together, the isothermal titration calorimetric and x-ray crystallographic results indicate that hydrogen bonding via interfacial water enthalpically contributes to the Fv-HEL interaction despite the partial offset because of entropy loss, suggesting that hydrogen bonding stiffens the antigen-antibody complex.

About this Structure

1J1X is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.

Reference

The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction., Yokota A, Tsumoto K, Shiroishi M, Kondo H, Kumagai I, J Biol Chem. 2003 Feb 14;278(7):5410-8. Epub 2002 Nov 19. PMID:12444085

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