1DEB

CRYSTAL STRUCTURE OF THE N-TERMINAL COILED COIL DOMAIN FROM APC

1DEB の概要

• エントリーDOI: 10.2210/pdb1deb/pdb
• 分子名称: ADENOMATOUS POLYPOSIS COLI PROTEIN, SULFATE ION (3 entities in total)
• 機能のキーワード: apc, coiled coil, tumor suppressor, structural protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell junction, adherens junction : P25054
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12315.71

構造登録者

Day, C.L.,Alber, T. (登録日: 1999-11-14, 公開日: 2000-09-06, 最終更新日: 2024-02-07)

主引用文献

Day, C.L.,Alber, T.
Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor.
J.Mol.Biol., 301:147-156, 2000

PubMed Abstract: Coiled coils serve as dimerization domains for a wide variety of proteins, including the medically important oligomeric tumor suppressor protein, APC. Mutations in the APC gene are associated with an inherited susceptibility to colon cancer and with approximately 75 % of sporadic colorectal tumors. To define the basis for APC pairing and to explore the anatomy of dimeric coiled coils, we determined the 2.4 A resolution X-ray crystal structure of the N-terminal dimerization domain of APC. The peptide APC-55, encompassing the heptad repeats in APC residues 2-55, primarily forms an alpha-helical, coiled-coil dimer with newly observed core packing features. Correlated asymmetric packing of four core residues in distinct, standard rotamers is associated with a small shift in the helix register. At the C terminus, the helices splay apart and interact with a symmetry-related dimer in the crystal to form a short, anti-parallel, four-helix bundle. N-terminal fraying and C-terminal splaying of the helices, as well as the asymmetry and helix register shift describe unprecedented dynamic excursions of coiled coils. The low stability of APC-55 and divergence from the expected coiled-coil fold support the suggestion that the APC dimerization domain may extend beyond the first 55 residues.

PubMed: 10926498
DOI: 10.1006/jmbi.2000.3895

実験手法

X-RAY DIFFRACTION (2.4 Å)