3T7U

A NeW Crystal structure of APC-ARM

Summary for 3T7U

• Entry DOI: 10.2210/pdb3t7u/pdb
• Descriptor: Adenomatous polyposis coli protein, PHOSPHATE ION (3 entities in total)
• Functional Keywords: armadillo repeats domain, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, adherens junction : P25054
• Total number of polymer chains: 2
• Total formula weight: 84286.57

Authors

Zhang, Z.,Wu, G. (deposition date: 2011-07-31, release date: 2011-12-14, Last modification date: 2023-11-01)

Primary citation

Zhang, Z.,Lin, K.,Gao, L.,Chen, L.,Shi, X.,Wu, G.
Crystal structure of the armadillo repeat domain of adenomatous polyposis coli which reveals its inherent flexibility
Biochem.Biophys.Res.Commun., 412:732-736, 2011

PubMed 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.

PubMed: 21871439
DOI: 10.1016/j.bbrc.2011.08.044

Experimental method

X-RAY DIFFRACTION (2.9 Å)