1j1o: Difference between revisions

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[[Image:1j1o.gif|left|200px]]<br />

[[Image:1j1o.gif|left|200px]]<br /><applet load="1j1o" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1j1o" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1j1o, resolution 1.8Å" />

'''Crystal Structure of HyHEL-10 Fv mutant LY50F complexed with hen egg white lysozyme'''<br />

==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.

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==

1J1O is a [http://en.wikipedia.org/wiki/Protein_complex 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]. Active as [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] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1J1O OCA].

1J1O is a [http://en.wikipedia.org/wiki/Protein_complex 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]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1O OCA].

==Reference==

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[[Category: antigen-antibody complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 18 09~~:33:~~31 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:59 2008''

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-[[Image:1j1o.gif|left|200px]]<br />
+[[Image:1j1o.gif|left|200px]]<br /><applet load="1j1o" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1j1o" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1j1o, resolution 1.8&Aring;" />
 '''Crystal Structure of HyHEL-10 Fv mutant LY50F complexed with hen egg white lysozyme'''<br />
 ==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.
+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==
-J1O is a [http://en.wikipedia.org/wiki/Protein_complex 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]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J1O OCA].
+J1O is a [http://en.wikipedia.org/wiki/Protein_complex 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]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1O OCA].
 ==Reference==
@@ Line 23: / Line 22: @@
 [[Category: antigen-antibody complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:33:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:59 2008''