This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1rjc

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rjc"

@@ Line 1: / Line 1: @@
-[[Image:1rjc.gif|left|200px]]<br />
-<applet load="1rjc" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1rjc, resolution 1.40&Aring;" />
-'''Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme'''<br />
-==Overview==
+==Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme==
-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.
+<StructureSection load='1rjc' size='340' side='right'caption='[[1rjc]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1rjc]] 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=1RJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJC FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1rjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rjc OCA], [https://pdbe.org/1rjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rjc RCSB], [https://www.ebi.ac.uk/pdbsum/1rjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rjc ProSAT]</span></td></tr>
+</table>
+== 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/rj/1rjc_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=1rjc ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-RJC is a [http://en.wikipedia.org/wiki/Single_protein 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] with PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RJC OCA].
+*[[Antibody 3D structures|Antibody 3D structures]]
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-==Reference==
+*[[3D structures of non-human antibody|3D structures of non-human antibody]]
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15659390 15659390]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Camelus dromedarius]]
 [[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: GOL]]
-[[Category: PO4]]
-[[Category: alpha-beta orthogonal bundle]]
-[[Category: beta sandwich]]
-[[Category: immunoglobulin fold]]
-[[Category: protein-protein hetero complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:41:23 2007''

1rjc

From Proteopedia

Current revision

Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox