2iak
From Proteopedia
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Crystal Structure of a protease resistant fragment of the plakin domain of Bullous Pemphigoid Antigen1 (BPAG1)
Overview
Bullous pemphigoid antigen 1 (BPAG1) is a member of the plakin family of, proteins. The plakins are multi-domain proteins that have been shown to, interact with microtubules, actin filaments and intermediate filaments, as, well as proteins found in cellular junctions. These interactions are, mediated through different domains on the plakins. The interactions, between plakins and components of specialized cell junctions such as, desmosomes and hemidesmosomes are mediated through the so-called plakin, domain, which is a common feature of the plakins. We report the crystal, structure of a stable fragment from BPAG1, residues 226-448, defined by, limited proteolysis of the whole plakin domain. The structure, determined, by single-wavelength anomalous diffraction phasing from a, selenomethionine-substituted crystal at 3.0 A resolution, reveals a tandem, pair of triple helical bundles closely related to spectrin repeats. Based, on this structure and analysis of sequence conservation, we propose that, the architecture of plakin domains is defined by two pairs of spectrin, repeats interrupted by a putative Src-Homology 3 (SH3) domain.
About this Structure
2IAK is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily., Jefferson JJ, Ciatto C, Shapiro L, Liem RK, J Mol Biol. 2007 Feb 9;366(1):244-57. Epub 2006 Nov 11. PMID:17161423
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