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[[Image:1jtp.gif|left|200px]]


{{Structure
==Degenerate interfaces in antigen-antibody complexes==
|PDB= 1jtp |SIZE=350|CAPTION= <scene name='initialview01'>1jtp</scene>, resolution 1.9&Aring;
<StructureSection load='1jtp' size='340' side='right'caption='[[1jtp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
<table><tr><td colspan='2'>[[1jtp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JTP FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1jtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jtp OCA], [https://pdbe.org/1jtp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jtp RCSB], [https://www.ebi.ac.uk/pdbsum/1jtp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jtp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSC_MELGA LYSC_MELGA] 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jt/1jtp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1jtp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In most of the work dealing with the analysis of protein-protein interfaces, a single X-ray structure is available or selected, and implicitly it is assumed that this structure corresponds to the optimal complex for this pair of proteins. However, we have found a degenerate interface in a high-affinity antibody-antigen complex: the two independent complexes of the camel variable domain antibody fragment cAb-Lys3 and its antigen hen egg white lysozyme present in the asymmetric unit of our crystals show a difference in relative orientation between antibody and antigen, leading to important differences at the protein-protein interface. A third cAb-Lys3-hen lysozyme complex in a different crystal form adopts yet another relative orientation. Our results show that protein-protein interface characteristics can vary significantly between different specimens of the same high-affinity antibody-protein antigen complex. Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics.


'''Degenerate interfaces in antigen-antibody complexes'''
Degenerate interfaces in antigen-antibody complexes.,Decanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L J Mol Biol. 2001 Oct 26;313(3):473-8. PMID:11676532<ref>PMID:11676532</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jtp" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
In most of the work dealing with the analysis of protein-protein interfaces, a single X-ray structure is available or selected, and implicitly it is assumed that this structure corresponds to the optimal complex for this pair of proteins. However, we have found a degenerate interface in a high-affinity antibody-antigen complex: the two independent complexes of the camel variable domain antibody fragment cAb-Lys3 and its antigen hen egg white lysozyme present in the asymmetric unit of our crystals show a difference in relative orientation between antibody and antigen, leading to important differences at the protein-protein interface. A third cAb-Lys3-hen lysozyme complex in a different crystal form adopts yet another relative orientation. Our results show that protein-protein interface characteristics can vary significantly between different specimens of the same high-affinity antibody-protein antigen complex. Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics.
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
==About this Structure==
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
1JTP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JTP OCA].
== References ==
 
<references/>
==Reference==
__TOC__
Degenerate interfaces in antigen-antibody complexes., Decanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L, J Mol Biol. 2001 Oct 26;313(3):473-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11676532 11676532]
</StructureSection>
[[Category: Camelus dromedarius]]
[[Category: Camelus dromedarius]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
[[Category: Protein complex]]
[[Category: Decanniere K]]
[[Category: Decanniere, K.]]
[[Category: Desmyter A]]
[[Category: Desmyter, A.]]
[[Category: Maes D]]
[[Category: Maes, D.]]
[[Category: Muyldermans S]]
[[Category: Muyldermans, S.]]
[[Category: Transue TR]]
[[Category: Transue, T R.]]
[[Category: Wyns L]]
[[Category: Wyns, L.]]
[[Category: FMT]]
[[Category: NA]]
[[Category: binding]]
[[Category: heavy chain antibody]]
[[Category: immunoglobulin]]
[[Category: interface]]
[[Category: vhh]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:08:18 2008''

Latest revision as of 11:45, 16 August 2023

Degenerate interfaces in antigen-antibody complexesDegenerate interfaces in antigen-antibody complexes

Structural highlights

1jtp is a 4 chain structure with sequence from Camelus dromedarius and Meleagris gallopavo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYSC_MELGA 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.

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

In most of the work dealing with the analysis of protein-protein interfaces, a single X-ray structure is available or selected, and implicitly it is assumed that this structure corresponds to the optimal complex for this pair of proteins. However, we have found a degenerate interface in a high-affinity antibody-antigen complex: the two independent complexes of the camel variable domain antibody fragment cAb-Lys3 and its antigen hen egg white lysozyme present in the asymmetric unit of our crystals show a difference in relative orientation between antibody and antigen, leading to important differences at the protein-protein interface. A third cAb-Lys3-hen lysozyme complex in a different crystal form adopts yet another relative orientation. Our results show that protein-protein interface characteristics can vary significantly between different specimens of the same high-affinity antibody-protein antigen complex. Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics.

Degenerate interfaces in antigen-antibody complexes.,Decanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L J Mol Biol. 2001 Oct 26;313(3):473-8. PMID:11676532[1]

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

See Also

References

  1. ↑ Decanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L. Degenerate interfaces in antigen-antibody complexes. J Mol Biol. 2001 Oct 26;313(3):473-8. PMID:11676532 doi:10.1006/jmbi.2001.5075

1jtp, resolution 1.90Å

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