2dqh: Difference between revisions

Revision as of 19:30, 27 July 2008

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File:2dqh.png

Template:STRUCTURE 2dqh

Crystal structure of hyhel-10 FV mutant (Hy58a) complexed with hen egg lysozymeCrystal structure of hyhel-10 FV mutant (Hy58a) complexed with hen egg lysozyme

Template:ABSTRACT PUBMED 17166830

About this StructureAbout this Structure

2DQH is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL., Shiroishi M, Tsumoto K, Tanaka Y, Yokota A, Nakanishi T, Kondo H, Kumagai I, J Biol Chem. 2007 Mar 2;282(9):6783-91. Epub 2006 Dec 12. PMID:17166830

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of hyhel-10 FV mutant (Hy58a) complexed with hen egg lysozyme'''
+===Crystal structure of hyhel-10 FV mutant (Hy58a) complexed with hen egg lysozyme===
-==Overview==
+<!--
-Tyrosine is an important amino acid in protein-protein interaction hot spots. In particular, many Tyr residues are located in the antigen-binding sites of antibodies and endow high affinity and high specificity to these antibodies. To investigate the role of interfacial Tyr residues in protein-protein interactions, we performed crystallographic studies and thermodynamic analyses of the interaction between hen egg lysozyme (HEL) and the anti-HEL antibody HyHEL-10 Fv fragment. HyHEL-10 has six Tyr residues in its antigen-binding site, which were systematically mutated to Phe and Ala using site-directed mutagenesis. The crystal structures revealed several critical roles for these Tyr residues in the interaction between HEL and HyHEL-10 as follows: 1) the aromatic ring of Tyr-50 in the light chain (LTyr-50) was important for the correct ternary structure of variable regions of the immunoglobulin light chain and heavy chain and of HEL; 2) deletion of the hydroxyl group of Tyr-50 in the heavy chain (HTyr-50) resulted in structural changes in the antigen-antibody interface; and 3) the side chains of HTyr-33 and HTyr-53 may help induce fitting of the antibody to the antigen. Hot spot Tyr residues may contribute to the high affinity and high specificity of the antigen-antibody interaction through a diverse set of structural and thermodynamic interactions.
+The line below this paragraph, {{ABSTRACT_PUBMED_17166830}}, adds the Publication Abstract to the page
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+-->
+{{ABSTRACT_PUBMED_17166830}}
 ==About this Structure==
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 [[Category: Immune system/hydrolase complex]]
 [[Category: Mutant]]
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