1RI8
Crystal Structure of the Camelid Single Domain Antibody 1D2L19 in complex with Hen Egg White Lysozyme
Summary for 1RI8
| Entry DOI | 10.2210/pdb1ri8/pdb |
| Descriptor | camelid ANTIBODY HEAVY CHAIN, Lysozyme C, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | beta sandwich, immunoglobulin fold, vhh-lysozyme complex, alpha-beta orthogonal bundle, immune system-hydrolase complex, immune system/hydrolase |
| Biological source | Camelus dromedarius (Arabian camel) More |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 2 |
| Total formula weight | 29140.53 |
| Authors | De Genst, E.,Silence, K.,Ghahroudi, M.A.,Decanniere, K.,Loris, R.,Kinne, J.,Wyns, L.,Muyldermans, S. (deposition date: 2003-11-17, release date: 2005-02-01, Last modification date: 2024-11-20) |
| Primary citation | De Genst, E.,Silence, K.,Ghahroudi, M.A.,Decanniere, K.,Loris, R.,Kinne, J.,Wyns, L.,Muyldermans, S. Strong in vivo maturation compensates for structurally restricted H3 loops in antibody repertoires. J.Biol.Chem., 280:14114-14121, 2005 Cited by PubMed Abstract: 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. PubMed: 15659390DOI: 10.1074/jbc.M413011200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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