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Crystal structure of the armadillo repeat domain of adenomatous polyposis coli which reveals its inherent flexibility.

Zhang Z, Lin K, Gao L, Chen L, Shi X, Wu G
Biochem Biophys Res Commun 412 732-6 (2011)
Cited: 12 times
EuropePMC logo PMID: 21871439

Abstract

The conserved armadillo repeat (ARM) domain of adenomatous polyposis coli (APC) protein plays an important role in the recognition of its binding partners. In this study, we report the crystal structure of APC-ARM (residues 407-775), which was determined to 2.9 Å resolution. Our structure shows that the seven armadillo repeats of APC-ARM fold together into a compact domain, with Arm2 and Arm5 presenting some deviations from canonical armadillo repeats. There is a positively charged groove on the surface of APC-ARM, which might be the recognition site for APC-binding partners. Comparison of this structure with our previously reported structure of APC (407-751), together with normal mode analysis, reveals that the APC-ARM domain possesses a limited intrinsic flexibility. We propose that this intrinsic flexibility might be an inherent property of ARM domains in general.

Reviews - 3t7u mentioned but not cited (1)

  1. The structural biology of canonical Wnt signalling. Agostino M, Pohl SÖ. Biochem Soc Trans 48 1765-1780 (2020)

Articles - 3t7u mentioned but not cited (1)

  1. The LRRK2 Variant E193K Prevents Mitochondrial Fission Upon MPP+ Treatment by Altering LRRK2 Binding to DRP1. Perez Carrion M, Pischedda F, Biosa A, Russo I, Straniero L, Civiero L, Guida M, Gloeckner CJ, Ticozzi N, Tiloca C, Mariani C, Pezzoli G, Duga S, Pichler I, Pan L, Landers JE, Greggio E, Hess MW, Goldwurm S, Piccoli G. Front Mol Neurosci 11 64 (2018)


Reviews citing this publication (2)

  1. Normal Mode Analysis as a Routine Part of a Structural Investigation. Bauer JA, Pavlović J, Bauerová-Hlinková V. Molecules 24 E3293 (2019)
  2. Advances and Insights of APC-Asef Inhibitors for Metastatic Colorectal Cancer Therapy. Yang X, Zhong J, Zhang Q, Feng L, Zheng Z, Zhang J, Lu S. Front Mol Biosci 8 662579 (2021)

Articles citing this publication (8)

  1. Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations. Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG. PLoS One 8 e77257 (2013)
  2. Structure of the nucleation-promoting factor SPIN90 bound to the actin filament nucleator Arp2/3 complex. Luan Q, Liu SL, Helgeson LA, Nolen BJ. EMBO J 37 e100005 (2018)
  3. A closed conformation of the Caenorhabditis elegans separase-securin complex. Bachmann G, Richards MW, Winter A, Beuron F, Morris E, Bayliss R. Open Biol 6 160032 (2016)
  4. Thermally-induced structural changes in an armadillo repeat protein suggest a novel thermosensor mechanism in a molecular chaperone. Bujalowski PJ, Nicholls P, Barral JM, Oberhauser AF. FEBS Lett 589 123-130 (2015)
  5. Structures of the APC-ARM domain in complexes with discrete Amer1/WTX fragments reveal that it uses a consensus mode to recognize its binding partners. Zhang Z, Akyildiz S, Xiao Y, Gai Z, An Y, Behrens J, Wu G. Cell Discov 1 15016 (2015)
  6. Truncated Adenomatous Polyposis Coli Mutation Induces Asef-Activated Golgi Fragmentation. Kim SB, Zhang L, Yoon J, Lee J, Min J, Li W, Grishin NV, Moon YA, Wright WE, Shay JW. Mol Cell Biol 38 e00135-18 (2018)
  7. Ric-8A, a GEF, and a Chaperone for G Protein α-Subunits: Evidence for the Two-Faced Interface. Srivastava D, Artemyev NO. Bioessays 42 e1900208 (2020)
  8. Structural Features of a Full-Length Ubiquitin Ligase Responsible for the Formation of Patches at the Plasma Membrane. Knop J, Lienemann T, El-Kilani H, Falke S, Krings C, Sindalovskaya M, Bergler J, Betzel C, Hoth S. Int J Mol Sci 22 9455 (2021)


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