4xos
ANP32A LRR domain
Structural highlights
FunctionAN32A_HUMAN Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression.[1] [2] [3] [4] Publication Abstract from PubMedAcidic leucine-rich nuclear phosphoprotein 32A (PP32A) is a tumour suppressor whose expression is altered in many cancers. It is an apoptotic enhancer that stimulates apoptosome-mediated caspase activation and also forms part of a complex involved in caspase-independent apoptosis (the SET complex). Crystals of a fragment of human PP32A corresponding to the leucine-rich repeat domain, a widespread motif suitable for protein-protein interactions, have been obtained. The structure has been refined to 1.56 A resolution. This domain was previously solved at 2.4 and 2.69 A resolution (PDB entries 2je0 and 2je1, respectively). The new high-resolution structure shows some differences from previous models: there is a small displacement in the turn connecting the first alpha-helix (alpha1) to the first beta-strand (beta1), which slightly changes the position of alpha1 in the structure. The shift in the turn is observed in the context of a new crystal packing unrelated to those of previous structures. High-resolution crystal structure of the leucine-rich repeat domain of the human tumour suppressor PP32A (ANP32A).,Zamora-Caballero S, Siauciunaite-Gaubard L, Bravo J Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):684-7. doi:, 10.1107/S2053230X15006457. Epub 2015 May 20. PMID:26057796[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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