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Domain organization of Mac-2 binding protein and its oligomerization to linear and ring-like structures.

Abstract：

:The multidomain Mac-2 binding protein (M2BP) is present in serum and in the extracellular matrix in the form of linear and ring-shaped oligomers, which interact with galectin-3, fibronectin, collagens, integrins and other large glycoproteins. Domain 1 of M2BP (M2BP-1) shows homology with the cysteine-rich SRCR domain of scavanger receptor. Domains 2 and 3 are related to the dimerization domains BTB/POZ and IVR of the Drosophila kelch protein. Recombinant M2BP, its N-terminal domain M2BP-1 and a fragment consisting of putative domains 2, 3 and 4 (M2BP-2,3,4) were investigated by scanning transmission electron microscopy, transmission electron microscopy, analytical ultracentrifugation and binding assays. The ring oligomers formed by the intact protein are comprised of approximately 14 nm long segments composed of two 92 kDa M2BP monomers. Although the rings vary in size, decamers predominate. The various linear oligomers also observed are probably ring precursors, dimers predominate. M2BP-1 exhibits a native fold, does not oligomerize and is inactive in cell attachment. M2BP-2,3,4 aggregates to heterogeneous, protein filled ring-like structures as shown by metal shadowed preparations. These aggregates retain the cell-adhesive potential indicating native folding. It is hypothesized that the rings provide an interaction pattern for multivalent interactions of M2BP with target molecules or complexes of ligands.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Müller SA,Sasaki T,Bork P,Wolpensinger B,Schulthess T,Timpl R,Engel A,Engel J

doi

10.1006/jmbi.1999.2996

keywords:

subject

Has Abstract

pub_date

1999-08-27 00:00:00

pages

801-13

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)92996-0

journal_volume

291

pub_type

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