2dqf: Difference between revisions

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[[Image:2dqf.png|left|200px]]


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==Crystal structure of hyhel-10 FV mutant (y33ay53a) complexed with hen egg lysozyme==
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<StructureSection load='2dqf' size='340' side='right'caption='[[2dqf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2dqf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DQF FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dqf OCA], [https://pdbe.org/2dqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dqf RCSB], [https://www.ebi.ac.uk/pdbsum/2dqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dqf ProSAT]</span></td></tr>
{{STRUCTURE_2dqf|  PDB=2dqf  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q65ZI1_MOUSE Q65ZI1_MOUSE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/2dqf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dqf ConSurf].
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== Publication Abstract from PubMed ==
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.


===Crystal structure of hyhel-10 FV mutant (y33ay53a) complexed with hen egg lysozyme===
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<ref>PMID:17166830</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2dqf" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17166830}}, adds the Publication Abstract to the page
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 17166830 is the PubMed ID number.
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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== References ==
{{ABSTRACT_PUBMED_17166830}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
2DQF 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=2DQF OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17166830 17166830]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Kondo H]]
[[Category: Kondo, H.]]
[[Category: Kumagai I]]
[[Category: Kumagai, I.]]
[[Category: Shiroishi M]]
[[Category: Shiroishi, M.]]
[[Category: Tsumoto K]]
[[Category: Tsumoto, K.]]
[[Category: Antigen-antibody complex]]
[[Category: Immune system/hydrolase complex]]
[[Category: Mutant]]
 
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