1j1p: Difference between revisions

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[[Image:1j1p.gif|left|200px]]
[[Image:1j1p.gif|left|200px]]


{{Structure
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
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{{STRUCTURE_1j1p| PDB=1j1p  | SCENE= }}  
|RELATEDENTRY=[[1c08|1C08]], [[1j1o|1J1O]], [[1j1x|1J1X]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j1p OCA], [http://www.ebi.ac.uk/pdbsum/1j1p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j1p RCSB]</span>
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'''Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme'''
'''Crystal structure of HyHEL-10 Fv mutant LS91A complexed with hen egg white lysozyme'''
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[[Category: Tsumoto, K.]]
[[Category: Tsumoto, K.]]
[[Category: Yokota, A.]]
[[Category: Yokota, A.]]
[[Category: antigen-antibody complex]]
[[Category: Antigen-antibody complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:41:50 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:27:39 2008''

Revision as of 20:41, 2 May 2008

File:1j1p.gif

Template:STRUCTURE 1j1p

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 Page seeded by OCA on Fri May 2 20:41:50 2008

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