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==Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme==
==Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme==
<StructureSection load='1j1x' size='340' side='right' caption='[[1j1x]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1j1x' size='340' side='right' caption='[[1j1x]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1j1x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick] 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=1J1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J1X FirstGlance]. <br>
<table><tr><td colspan='2'>[[1j1x]] 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=1J1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J1X 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]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c08|1c08]], [[1j1o|1j1o]], [[1j1p|1j1p]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j1x OCA], [http://pdbe.org/1j1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j1x RCSB], [http://www.ebi.ac.uk/pdbsum/1j1x PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j1x OCA], [http://pdbe.org/1j1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j1x RCSB], [http://www.ebi.ac.uk/pdbsum/1j1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j1x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j1/1j1x_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j1/1j1x_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 31: Line 32:
==See Also==
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
*[[Monoclonal Antibody|Monoclonal Antibody]]
*[[3D structures of monoclonal antibody|3D structures of monoclonal antibody]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chick]]
[[Category: Gallus gallus]]
[[Category: Lk3 transgenic mice]]
[[Category: Lk3 transgenic mice]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]

Revision as of 11:58, 17 January 2018

Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozymeCrystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme

Structural highlights

1j1x is a 3 chain structure with sequence from Gallus gallus and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:Lysozyme, with EC number 3.2.1.17
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

To study the role of hydrogen bonding via interfacial water molecules in protein-protein interactions, we examined the interaction between hen egg white lysozyme (HEL) and its HyHEL-10 variable domain fragment (Fv) antibody. We constructed three antibody mutants (l-Y50F, l-S91A, and l-S93A) and investigated the interactions between the mutant Fvs and HEL. Isothermal titration calorimetry indicated that the mutations significantly decreased the negative enthalpy change (8-25 kJ mol(-1)), despite some offset by a favorable entropy change. X-ray crystallography demonstrated that the complexes had nearly identical structures, including the positions of the interfacial water molecules. Taken together, the isothermal titration calorimetric and x-ray crystallographic results indicate that hydrogen bonding via interfacial water enthalpically contributes to the Fv-HEL interaction despite the partial offset because of entropy loss, suggesting that hydrogen bonding stiffens the antigen-antibody complex.

The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction.,Yokota A, Tsumoto K, Shiroishi M, Kondo H, Kumagai I J Biol Chem. 2003 Feb 14;278(7):5410-8. Epub 2002 Nov 19. PMID:12444085[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. 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
  2. Yokota A, Tsumoto K, Shiroishi M, Kondo H, Kumagai I. The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction. J Biol Chem. 2003 Feb 14;278(7):5410-8. Epub 2002 Nov 19. PMID:12444085 doi:http://dx.doi.org/10.1074/jbc.M210182200

1j1x, resolution 1.80Å

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