1j1p: Difference between revisions
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'''Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme''' | {{Structure | ||
|PDB= 1j1p |SIZE=350|CAPTION= <scene name='initialview01'>1j1p</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= | |||
|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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1J1P is a [ | 1J1P is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1P OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12444085 12444085] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: antigen-antibody complex]] | [[Category: antigen-antibody complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:57:49 2008'' | ||
Revision as of 12:57, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme
OverviewOverview
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 StructureAbout this Structure
1J1P is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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