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[[Image:1ri8.gif|left|200px]]


{{Structure
==Crystal Structure of the Camelid Single Domain Antibody 1D2L19 in complex with Hen Egg White Lysozyme==
|PDB= 1ri8 |SIZE=350|CAPTION= <scene name='initialview01'>1ri8</scene>, resolution 1.85&Aring;
<StructureSection load='1ri8' size='340' side='right'caption='[[1ri8]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[1ri8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RI8 FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ri8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ri8 OCA], [https://pdbe.org/1ri8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ri8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ri8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ri8 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ri8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ri8 OCA], [http://www.ebi.ac.uk/pdbsum/1ri8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ri8 RCSB]</span>
== Function ==
}}
[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 ==
[[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/ri/1ri8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ri8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A central paradigm in immunology states that successful generation of high affinity antibodies necessitates an immense primary repertoire of antigen-combining sites. Much of the diversity of this repertoire is provided by varying one antigen binding loop, created by inserting randomly a D (diversity) gene out of a small pool between the V and J genes. It is therefore assumed that any particular D-encoded region surrounded by different V and J regions adopts a different conformation. We have solved the structure of two lysozyme-specific variable domains of heavy-chain antibodies isolated from two strictly unrelated dromedaries. These antibodies recombined identical D gene sequences to different V and J precursors with significant variance in their V(D)J junctions. Despite these large differences, the D-encoded loop segments adopt remarkably identical architectures, thus directing the antibodies toward identical epitopes. Furthermore, a striking convergent maturation process occurred in the V region, adapting both binders for their sub-nanomolar affinity association with lysozyme. Hence, on a structural level, humoral immunity may rely more on well developed maturation and selection systems than on the acquisition of large primary repertoires.


'''Crystal Structure of the Camelid Single Domain Antibody 1D2L19 in complex with Hen Egg White Lysozyme'''
Strong in vivo maturation compensates for structurally restricted H3 loops in antibody repertoires.,De Genst E, Silence K, Ghahroudi MA, Decanniere K, Loris R, Kinne J, Wyns L, Muyldermans S J Biol Chem. 2005 Apr 8;280(14):14114-21. Epub 2005 Jan 19. PMID:15659390<ref>PMID:15659390</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ri8" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
A central paradigm in immunology states that successful generation of high affinity antibodies necessitates an immense primary repertoire of antigen-combining sites. Much of the diversity of this repertoire is provided by varying one antigen binding loop, created by inserting randomly a D (diversity) gene out of a small pool between the V and J genes. It is therefore assumed that any particular D-encoded region surrounded by different V and J regions adopts a different conformation. We have solved the structure of two lysozyme-specific variable domains of heavy-chain antibodies isolated from two strictly unrelated dromedaries. These antibodies recombined identical D gene sequences to different V and J precursors with significant variance in their V(D)J junctions. Despite these large differences, the D-encoded loop segments adopt remarkably identical architectures, thus directing the antibodies toward identical epitopes. Furthermore, a striking convergent maturation process occurred in the V region, adapting both binders for their sub-nanomolar affinity association with lysozyme. Hence, on a structural level, humoral immunity may rely more on well developed maturation and selection systems than on the acquisition of large primary repertoires.
*[[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]]
1RI8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RI8 OCA].
== References ==
 
<references/>
==Reference==
__TOC__
Strong in vivo maturation compensates for structurally restricted H3 loops in antibody repertoires., De Genst E, Silence K, Ghahroudi MA, Decanniere K, Loris R, Kinne J, Wyns L, Muyldermans S, J Biol Chem. 2005 Apr 8;280(14):14114-21. Epub 2005 Jan 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15659390 15659390]
</StructureSection>
[[Category: Camelus dromedarius]]
[[Category: Camelus dromedarius]]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: De Genst E]]
[[Category: Decanniere, K.]]
[[Category: Decanniere K]]
[[Category: Genst, E De.]]
[[Category: Ghahroudi MA]]
[[Category: Ghahroudi, M A.]]
[[Category: Kinne J]]
[[Category: Kinne, J.]]
[[Category: Loris R]]
[[Category: Loris, R.]]
[[Category: Muyldermans S]]
[[Category: Muyldermans, S.]]
[[Category: Silence K]]
[[Category: Silence, K.]]
[[Category: Wyns L]]
[[Category: Wyns, L.]]
[[Category: alpha-beta orthogonal bundle]]
[[Category: beta sandwich]]
[[Category: immunoglobulin fold]]
[[Category: vhh-lysozyme complex]]
 
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