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Multimerization potential of the cytoplasmic domain of the human cytomegalovirus glycoprotein B
Author(s) -
Scheffczik Hanno,
Kraus Ina,
Kiermayer Simone,
Bogner Elke,
Holzenburg Andreas,
Garten Wolfgang,
Eickmann Markus
Publication year - 2001
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/s0014-5793(01)02891-5
Subject(s) - homotetramer , cytoplasm , circular dichroism , glycoprotein , recombinant dna , chemistry , human cytomegalovirus , protein secondary structure , gel permeation chromatography , microbiology and biotechnology , biology , biophysics , biochemistry , gene , organic chemistry , protein subunit , polymer
In the present study the coding sequence of the cytoplasmic tail of the human cytomegalovirus glycoprotein B (gB) was expressed. The secondary structure of the purified recombinant protein was analyzed by circular dichroism, and the quaternary structure was investigated by gel permeation chromatography, and electron microscopy. Our data indicate that the cytoplasmic gB domain contains α‐helix structures and assembles into tetramers, suggesting that the authentic gB may represent a homotetramer.