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The solution structure of an N‐terminally truncated version of the yeast CDC24p PB1 domain shows a different β‐sheet topology
Author(s) -
Leitner Dietmar,
Wahl Martin,
Labudde Dirk,
Krause Gerd,
Diehl Anne,
Schmieder Peter,
Pires José Ricardo,
Fossi Michele,
Wiedemann Urs,
Leidert Martina,
Oschkinat Hartmut
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.025
Subject(s) - guanine nucleotide exchange factor , yeast , topology (electrical circuits) , microbiology and biotechnology , cell division , c terminus , budding yeast , saccharomyces cerevisiae , biology , chemistry , cell , genetics , signal transduction , amino acid , mathematics , combinatorics
Phox and Bem1 (PB1) domains mediate protein–protein interactions via the formation of homo‐ or hetero‐dimers. The C‐terminal PB1 domain of yeast cell division cycle 24 (CDC24p), a guanine‐nucleotide exchange factor involved in cell polarity establishment, is known to interact with the PB1 domain occurring in bud emergence MSB1 interacting 1 (BEM1p) during the regulation of the yeast budding process via its OPR/PC/AID (OPCA) motif. Here, we present the structure of an N‐terminally truncated version of the Sc CDC24p PB1 domain. It shows a different topology of the β‐sheet than the long form. However, the C‐terminal part of the structure shows the conserved PB1 domain features including the OPCA motif with a slight rearrangement of helix α1. Residues which are important for the heterodimerization with BEM1p are structurally preserved.