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Surface recognition elements of membrane protein oligomerization
Author(s) -
Rath Arianna,
Deber Charles M.
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21569
Subject(s) - protein quaternary structure , membrane , membrane protein , monomer , structural motif , sequence (biology) , protein structure , peptide sequence , peripheral membrane protein , chemistry , biochemistry , biophysics , protein subunit , biology , integral membrane protein , organic chemistry , gene , polymer
Although certain membrane proteins are functional as monomeric polypeptides, others must assemble into oligomers to carry out their biological roles. High‐resolution membrane protein structures provide a valuable resource for examining the sequence features that facilitate—or preclude—assembly of membrane protein monomers into multimeric structures. Here we have utilized a data set of 28 high‐resolution α‐helical membrane protein structures comprising 32 nonredundant polypeptides to address this issue. The lipid‐exposed surfaces of membrane proteins that have reached their fully assembled and functional biological units have been compared with those of the individual subunits that build quaternary structures. Though the overall amino acid composition of each set of surfaces is similar, a key distinction—the distribution of small‐xxx‐small motifs—delineates subunits from membrane proteins that have reached a functioning oligomeric state. Quaternary structure formation may therefore be dictated by small‐xxx‐small motifs that are not satisfied by intrachain contacts. Proteins 2008. © 2007 Wiley‐Liss, Inc.