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High‐resolution crystal structure of the leucine‐rich repeat domain of the human tumour suppressor PP32A (ANP32A)
Author(s) -
ZamoraCaballero Sara,
ŠiaučiunaiteGaubard Lina,
Bravo Jeronimo
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15006457
Subject(s) - leucine zipper , protein data bank (rcsb pdb) , leucine rich repeat , context (archaeology) , leucine , phosphoprotein , crystal structure , suppressor , resolution (logic) , enhancer , biology , chemistry , crystallography , microbiology and biotechnology , amino acid , peptide sequence , stereochemistry , genetics , transcription factor , kinase , computer science , gene , paleontology , artificial intelligence
Acidic 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 Å resolution. This domain was previously solved at 2.4 and 2.69 Å 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 α‐helix (α1) to the first β‐strand (β1), which slightly changes the position of α1 in the structure. The shift in the turn is observed in the context of a new crystal packing unrelated to those of previous structures.