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| <StructureSection load='6p4d' size='340' side='right'caption='[[6p4d]], [[Resolution|resolution]] 1.05Å' scene=''> | | <StructureSection load='6p4d' size='340' side='right'caption='[[6p4d]], [[Resolution|resolution]] 1.05Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6p4d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P4D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6P4D FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P4D FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.05Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LYZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6p4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p4d OCA], [https://pdbe.org/6p4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p4d RCSB], [https://www.ebi.ac.uk/pdbsum/6p4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p4d ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6p4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p4d OCA], [http://pdbe.org/6p4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p4d RCSB], [http://www.ebi.ac.uk/pdbsum/6p4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p4d ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function ==
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| [[http://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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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Conformational diversity and self-cross-reactivity of antigens have been correlated with evasion from neutralizing antibody responses. We utilized single cell B cell sequencing, biolayer interferometry and X-ray crystallography to trace mutation selection pathways where the antibody response must resolve cross-reactivity between foreign and self-proteins bearing near-identical contact surfaces, but differing in conformational flexibility. Recurring antibody mutation trajectories mediate long-range rearrangements of framework (FW) and complementarity determining regions (CDRs) that increase binding site conformational diversity. These antibody mutations decrease affinity for self-antigen 19-fold and increase foreign affinity 67-fold, to yield a more than 1,250-fold increase in binding discrimination. These results demonstrate how conformational diversity in antigen and antibody does not act as a barrier, as previously suggested, but rather facilitates high affinity and high discrimination between foreign and self.
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| Conformational diversity facilitates antibody mutation trajectories and discrimination between foreign and self-antigens.,Burnett DL, Schofield P, Langley DB, Jackson J, Bourne K, Wilson E, Porebski BT, Buckle AM, Brink R, Goodnow CC, Christ D Proc Natl Acad Sci U S A. 2020 Sep 8;117(36):22341-22350. doi:, 10.1073/pnas.2005102117. Epub 2020 Aug 27. PMID:32855302<ref>PMID:32855302</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6p4d" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Lysozyme 3D structures|Lysozyme 3D structures]] | | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Chick]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Lysozyme]]
| | [[Category: Christ D]] |
| [[Category: Christ, D]] | | [[Category: Langley DB]] |
| [[Category: Langley, D B]] | |
| [[Category: Hen egg lysozyme hel3x]]
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| [[Category: Hydrolase]]
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