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| | <StructureSection load='3a6c' size='340' side='right'caption='[[3a6c]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='3a6c' size='340' side='right'caption='[[3a6c]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a6c]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A6C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a6c]] 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=3A6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A6C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c08|1c08]], [[1j1o|1j1o]], [[1j1p|1j1p]], [[1j1x|1j1x]], [[2dqi|2dqi]], [[2dqj|2dqj]], [[3a67|3a67]], [[3a6b|3a6b]]</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]] 1.8Å</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=3a6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6c OCA], [https://pdbe.org/3a6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a6c RCSB], [https://www.ebi.ac.uk/pdbsum/3a6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6c 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=3a6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6c OCA], [http://pdbe.org/3a6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a6c RCSB], [http://www.ebi.ac.uk/pdbsum/3a6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Kondo H]] |
| - | [[Category: Kondo, H]] | + | [[Category: Kumagai I]] |
| - | [[Category: Kumagai, I]] | + | [[Category: Nakanishi T]] |
| - | [[Category: Nakanishi, T]] | + | [[Category: Shiroishi M]] |
| - | [[Category: Shiroishi, M]] | + | [[Category: Tsumoto K]] |
| - | [[Category: Tsumoto, K]] | + | [[Category: Yokota A]] |
| - | [[Category: Yokota, A]] | + | |
| - | [[Category: Allergen]]
| + | |
| - | [[Category: Antigen-antibody complex]]
| + | |
| - | [[Category: Antimicrobial]]
| + | |
| - | [[Category: Bacteriolytic enzyme]]
| + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Immune system-hydrolase complex]]
| + | |
| - | [[Category: Mutant]]
| + | |
| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Many germ line antibodies have asparagine residues at specific sites to achieve specific antigen recognition. To study the role of asparagine residues in the stabilization of antigen-antibody complexes, we examined the interaction between hen egg white lysozyme (HEL) and the corresponding HyHEL-10 variable domain fragment (Fv). We introduced Ala and Asp substitutions into the Fv side chains of L-Asn-31, L-Asn-32, and L-Asn-92, which interact directly with residues in HEL via hydrogen bonding in the wild-type Fv-HEL complex, and we investigated the interactions between these mutant antibodies and HEL. Isothermal titration calorimetric analysis showed that all the mutations decreased the negative enthalpy change and decreased the association constants of the interaction. Structural analyses showed that the effects of the mutations on the structure of the complex could be compensated for by conformational changes and/or by gains in other interactions. Consequently, the contribution of two hydrogen bonds was minor, and their abolition by mutation resulted in only a slight decrease in the affinity of the antibody for its antigen. By comparison, the other two hydrogen bonds buried at the interfacial area had large enthalpic advantage, despite entropic loss that was perhaps due to stiffening of the interface by the bonds, and were crucial to the strength of the interaction. Deletion of these strong hydrogen bonds could not be compensated for by other structural changes. Our results suggest that asparagine can provide the two functional groups for strong hydrogen bond formation, and their contribution to the antigen-antibody interaction can be attributed to their limited flexibility and accessibility at the complex interface.
Contribution of asparagine residues to the stabilization of a proteinaceous antigen-antibody complex, HyHEL-10-hen egg white lysozyme.,Yokota A, Tsumoto K, Shiroishi M, Nakanishi T, Kondo H, Kumagai I J Biol Chem. 2010 Mar 5;285(10):7686-96. Epub 2009 Dec 28. PMID:20038580[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
- ↑ Yokota A, Tsumoto K, Shiroishi M, Nakanishi T, Kondo H, Kumagai I. Contribution of asparagine residues to the stabilization of a proteinaceous antigen-antibody complex, HyHEL-10-hen egg white lysozyme. J Biol Chem. 2010 Mar 5;285(10):7686-96. Epub 2009 Dec 28. PMID:20038580 doi:10.1074/jbc.M109.089623
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