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Crystal structure of metastasis-associated protein S100A4 in the active calcium-bound form.

Abstract：

:S100A4 (metastasin) is a member of the S100 family of calcium-binding proteins that is directly involved in tumorigenesis. Until recently, the only structural information available was the solution NMR structure of the inactive calcium-free form of the protein. Here we report the crystal structure of human S100A4 in the active calcium-bound state at 2.03 A resolution that was solved by molecular replacement in the space group P6(5) with two molecules in the asymmetric unit from perfectly merohedrally twinned crystals. The Ca(2+)-bound S100A4 structure reveals a large conformational change in the three-dimensional structure of the dimeric S100A4 protein upon calcium binding. This calcium-dependent conformational change opens up a hydrophobic binding pocket that is capable of binding to target proteins such as annexin A2, the tumor-suppressor protein p53 and myosin IIA. The structure of the active form of S100A4 provides insight into its interactions with its binding partners and a better understanding of its role in metastasis.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Pathuri P,Vogeley L,Luecke H

doi

10.1016/j.jmb.2008.04.076

subject

Has Abstract

pub_date

2008-10-31 00:00:00

pages

62-77

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(08)00542-1

journal_volume

383

pub_type

杂志文章

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