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Human FLJ10324 (RADIL), RA domain

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PDB Code 3EC8 Target Class Cell-type specific expression Target FLJ10324 Alias n/a Disease Area/Function Date Deposited Aug 29 2008 Authors Wisniewska, M., Lehtio, L., Andersson, J., Arrowsmith, C.H., Berglund, H., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Johansson, A., Johansson, I., Karlberg, T., Kotenyova, T., Moche, M., Nilsson, M.E., Nordlund, P., Nyman, T., Olesen, K., Persson, C., Sagemark, J., Schueler, H., Thorsell, A.G., Tresaugues, L., van den Berg, S., Weigelt, J., Welin, M., Wikstrom, M., Berglund, H.

About this structure

FLJ10324 (also called RADIL, KIAA1849, AF6L) is a multi-domain protein composed of a Ras association (RA) domain, a forkhead-associated (FHA) domain mediating phospho-peptide interactions, a dilute (DIL domain) of unknown function, and a protein-protein interacting PDZ domain.

The RA domain is structurally similar to ubiquitin and is present in one or two copies in a number of signalling molecules that bind and regulate a small GTPase called Ras or the Ras-related GTPases, Ral and Rap. RA-containing proteins include RalGDS, AF6, RIN1, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.

At date there is limited knowledge about the specific biological role played by FLJ10342. This protein has a similar domain composition as afadin (AF6), a protein involved in linking membrane-associated proteins to the actin cytoskeleton and in Rap-induced cell adhesion that suggests a related role for FLJ10324.

The RA domain of FLJ10324 has been shown to bind to the small GTPase Rap1 and reduce the exchange rate of the nucleotide but seems not to effect Rap-induced cell adhesion in a similar way as afadin (1). Later FLJ10324 has been shown to be required for cell adhesion and migration of neural crest precursors, a highly motile embryonic cell population that give rise to different cell types (2).

Here we present the crystal structure of RA domain of FLJ10324 at 2.6Å resolution. The structure was solved by MIRAS phasing using heavy atoms derivatives (lead and mercury). The overall structure reveals the ubiquitin-like fold consisting of five-stranded β-sheet and two α-helices. Additionally, at N- and C- terminus we can observe two α-helices that do not belong to the RA domain.

References

  1. AF6 negatively regulates Rap1-induced cell adhesion. Zhang et al JBC 20005, 280, 33200-33205
  2. A Rap GTPase interactor, RADIL, mediates migration of neural crest precursors. Smolen et al Genes and Development 2007, 21, 2131-2136