1xgp

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[[Image:1xgp.gif|left|200px]]
 
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{{Structure
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==Structure for antibody HyHEL-63 Y33A mutant complexed with hen egg lysozyme==
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|PDB= 1xgp |SIZE=350|CAPTION= <scene name='initialview01'>1xgp</scene>, resolution 2.10&Aring;
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<StructureSection load='1xgp' size='340' side='right'caption='[[1xgp]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1xgp]] 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=1XGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XGP FirstGlance]. <br>
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|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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</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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|GENE=
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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=1xgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xgp OCA], [https://pdbe.org/1xgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xgp RCSB], [https://www.ebi.ac.uk/pdbsum/1xgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xgp ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xgp OCA], [http://www.ebi.ac.uk/pdbsum/1xgp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xgp RCSB]</span>
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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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}}
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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/1xgp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1xgp 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 Y33A 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 1xgp" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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==About this Structure==
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== References ==
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1XGP is a [[Single protein]] structure of sequence 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=1XGP OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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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: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Li Y]]
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[[Category: Li, Y.]]
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[[Category: Mariuzza RA]]
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[[Category: Mariuzza, R A.]]
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[[Category: 2 1a resolution]]
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[[Category: hyhel-63]]
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[[Category: y33a mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:49:23 2008''
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Current revision

Structure for antibody HyHEL-63 Y33A mutant complexed with hen egg lysozyme

PDB ID 1xgp

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