5WK4

Crystal structure of an anti-idiotype VLR

Summary for 5WK4

• Entry DOI: 10.2210/pdb5wk4/pdb
• Descriptor: Variable lymphocyte receptor 39, MAGNESIUM ION (3 entities in total)
• Functional Keywords: leucine-rich repeat antibody antigen receptor, immune system
• Biological source: Petromyzon marinus (Sea lamprey)
• Total number of polymer chains: 6
• Total formula weight: 131850.34

Authors

Collins, B.C.,Nakahara, H.,Cooper, M.D.,Herrin, B.R.,Wilson, I.A. (deposition date: 2017-07-24, release date: 2017-12-13, Last modification date: 2024-10-30)

Primary citation

Collins, B.C.,Nakahara, H.,Acharya, S.,Cooper, M.D.,Herrin, B.R.,Wilson, I.A.
Crystal structure of an anti-idiotype variable lymphocyte receptor.
Acta Crystallogr F Struct Biol Commun, 73:682-687, 2017

PubMed Abstract: Variable lymphocyte receptors (VLRs), the leucine-rich repeat (LRR)-based antigen receptors of jawless fish, have great utility in a wide variety of biochemical and biological applications, similar to classical Ig-based antibodies. VLR-based reagents may be particularly useful when traditional antibodies are not available. An anti-idiotype lamprey VLR, VLR39, has previously been identified that recognizes the heavy-chain CDR3 of the B-cell receptor (BCR) of a leukemic clone from a patient with chronic lymphocytic leukemia (CLL). VLR39 was used successfully to track the re-emergence of this clone in the patient following chemotherapy. Here, the crystal structure of VLR39 is presented at 1.5 Å resolution and compared with those of other protein-specific VLRs. VLR39 adopts a curved solenoid fold and exhibits substantial structural similarity to other protein-binding VLRs. VLR39 has a short LRRCT loop that protrudes outwards away from the concave face and is similar to those of its protein-specific VLR counterparts. Analysis of the VLR39-BCR interaction by size-exclusion chromatography and biolayer interferometry using the scFv version of the BCR confirms that VLR39 recognizes the BCR Fv region. Such VLR-based reagents may be useful for identifying and monitoring leukemia in CLL patients and in other clinical diagnostic assays.

PubMed: 29199989
DOI: 10.1107/S2053230X1701620X

Experimental method

X-RAY DIFFRACTION (1.498 Å)