1xgu

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{{Seed}}
 
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[[Image:1xgu.png|left|200px]]
 
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==Structure for antibody HyHEL-63 Y33F mutant complexed with hen egg lysozyme==
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The line below this paragraph, containing "STRUCTURE_1xgu", creates the "Structure Box" on the page.
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<StructureSection load='1xgu' size='340' side='right'caption='[[1xgu]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1xgu]] is a 3 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=1XGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XGU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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=1xgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xgu OCA], [https://pdbe.org/1xgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xgu RCSB], [https://www.ebi.ac.uk/pdbsum/1xgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xgu ProSAT]</span></td></tr>
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{{STRUCTURE_1xgu| PDB=1xgu | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xg/1xgu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1xgu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hydrophobic interactions are essential for stabilizing protein-protein complexes, whose interfaces generally consist of a central cluster of hot spot residues surrounded by less important peripheral residues. According to the O-ring hypothesis, a condition for high affinity binding is solvent exclusion from interacting residues. This hypothesis predicts that the hydrophobicity at the center is significantly greater than at the periphery, which we estimated at 21 cal mol(-1) A(-2). To measure the hydrophobicity at the center, structures of an antigen-antibody complex where a buried phenylalanine was replaced by smaller hydrophobic residues were determined. By correlating structural changes with binding free energies, we estimate the hydrophobicity at this central site to be 46 cal mol(-1) A(-2), twice that at the periphery. This context dependence of the hydrophobic effect explains the clustering of hot spots at interface centers and has implications for hot spot prediction and the design of small molecule inhibitors.
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===Structure for antibody HyHEL-63 Y33F mutant complexed with hen egg lysozyme===
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Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces.,Li Y, Huang Y, Swaminathan CP, Smith-Gill SJ, Mariuzza RA Structure. 2005 Feb;13(2):297-307. PMID:15698573<ref>PMID:15698573</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1xgu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15698573}}, adds the Publication Abstract to the page
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15698573 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15698573}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Gallus gallus]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGU OCA].
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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==Reference==
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[[Category: Huang Y]]
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Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces., Li Y, Huang Y, Swaminathan CP, Smith-Gill SJ, Mariuzza RA, Structure. 2005 Feb;13(2):297-307. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15698573 15698573]
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[[Category: Li Y]]
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[[Category: 2 1a crystal structure]]
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[[Category: Mariuzza RA]]
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[[Category: Hyhel-63]]
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[[Category: Smith-Gill SJ]]
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[[Category: Y33f mutant]]
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[[Category: Swaminathan CP]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:52:32 2008''
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Current revision

Structure for antibody HyHEL-63 Y33F mutant complexed with hen egg lysozyme

PDB ID 1xgu

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