Seroatlas · Protein domains

Butyrophylin-like, SPRY domain

IPR003879

Definition

Several proteins that contain RING fingers also contain a well-conserved 40-residue cysteine-rich domain termed a B-box zinc finger. Often, one or two copies of the B-box are associated with a coiled coil domain ([interpro:IPR003649]) in addition to the ring finger ([interpro:IPR001841]), forming a tripartite motif. The tripartite motif is found in transcription factors, ribonucleoproteins and proto-oncoproteins, but no function has yet been ascribed to the domain PMID:9923704. The solution structure of the B-box motif has been determined by NMR. The protein is a monomer, with 2 β-strands, 2 helical turns and 3 extended loop regions packed in a novel topology PMID:8846787. Of 7 potential zinc ligands, only 4 are used, binding a single zinc atom in a C2-H2 tetrahedral arrangement. The B-box structure differs in tertiary fold from all other known zinc-binding motifs. A group of proteins that contain the B-box motif also host a well conserved domain of unknown function. Proteins that include this domain are, e.g.: butyrophilin, the RET finger protein, the 52kDa Ro protein and the Xenopus nuclear factor protein. The C-terminal portion of this region has been termed the SPRY domain (after SPla and the RYanodine Receptor) PMID:9923704.

70 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

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