期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 279, 期 16, 页码 16591-16597出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M313936200
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资金
- NIGMS NIH HHS [GM063919, R01 GM063919-05, R01 GM063919-04, R01 GM063919-08, R01 GM063919-07, GM54160, R01 GM063919, R01 GM063919-06] Funding Source: Medline
Sequence motifs are responsible for ensuring the proper assembly of transmembrane (TM) helices in the lipid bilayer. To understand the mechanism by which the affinity of a common TM-TM interactive motif is controlled at the sequence level, we compared two well characterized GXXXG motif-containing homodimers, those formed by human erythrocyte protein glycophorin A (GpA, high-affinity dimer) and those formed by bacteriophage M13 major coat protein (MCP, low affinity dimer). In both constructs, the GXXXG motif is necessary for TM-TM association. Although the remaining interfacial residues (underlined) in GpA ((LI) under bar XXG (V) under bar XXG (V) under bar XX (T) under bar) differ from those in MCP ( (VV) under bar XXG (A) under bar XXG (I) under bar XX (F) under bar), molecular modeling performed here indicated that GpA and MCP dimers possess the same overall fold. Thus, we could introduce GpA interfacial residues, alone and in combination, into the MCP sequence to help decrypt the determinants of dimer affinity. Using both in vivo TOXCAT assays and SDS-PAGE gel migration rates of synthetic peptides derived from TM regions of the proteins, we found that the most distal interfacial sites, 12 residues apart (and similar to18 Angstrom in structural space), work in concert to control TM-TM affinity synergistically.
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