1rjc
From Proteopedia
(New page: 200px<br /> <applet load="1rjc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rjc, resolution 1.40Å" /> '''Crystal structure o...) |
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| - | [[Image:1rjc.gif|left|200px]]<br /> | + | [[Image:1rjc.gif|left|200px]]<br /><applet load="1rjc" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rjc" size=" | + | |
caption="1rjc, resolution 1.40Å" /> | caption="1rjc, resolution 1.40Å" /> | ||
'''Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme'''<br /> | '''Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A central paradigm in immunology states that successful generation of high | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1RJC 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:// | + | 1RJC 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 <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Decanniere, K.]] | [[Category: Decanniere, K.]] | ||
| - | [[Category: Genst, E | + | [[Category: Genst, E De.]] |
| - | [[Category: Ghahroudi, M | + | [[Category: Ghahroudi, M A.]] |
[[Category: Kinne, J.]] | [[Category: Kinne, J.]] | ||
[[Category: Loris, R.]] | [[Category: Loris, R.]] | ||
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[[Category: protein-protein hetero complex]] | [[Category: protein-protein hetero complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:30 2008'' |
Revision as of 12:51, 21 February 2008
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Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme
Overview
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.
About this Structure
1RJC is a Single protein structure of sequence from Camelus dromedarius and Gallus gallus with and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:51:30 2008
Categories: Camelus dromedarius | Gallus gallus | Lysozyme | Single protein | Decanniere, K. | Genst, E De. | Ghahroudi, M A. | Kinne, J. | Loris, R. | Muyldermans, S. | Silence, K. | Wyns, L. | GOL | PO4 | Alpha-beta orthogonal bundle | Beta sandwich | Immunoglobulin fold | Protein-protein hetero complex
