Temperature-induced formation of a non-native intermediate state of the all beta-sheet protein CD2

Domain 1 of the cell adhesion protein CD2 (CD2-1) has an all beta-structure typical of proteins belonging to the immunoglobin superfamily. It has a remarkable ability to fold as a native monomer or a metastable intertwined dimer. To understand the origin of structural rearrangements of CD2-1, we hav...

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Bibliographic Details
Published in:Cell biochemistry and biophysics 2002-01, Vol.36 (1), p.1-18
Main Authors: Yang, Jenny J, Yang, Haidong, Ye, Yiming, Hopkins, Jr, Harry, Hastings, Gary
Format: Article
Language:English
Subjects:
Amino acid sequence
Anilino Naphthalenesulfonates - pharmacology
Animals
CD2 Antigens - chemistry
Cell adhesion
Coils
Dimerization
Domains
Ellipticity
Escherichia coli - metabolism
Fluorescent Dyes
Genetic Vectors
High temperature
Hydrophobicity
Infrared Rays
Plasmids - metabolism
Protein Conformation
Protein Denaturation
Protein folding
Protein structure
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Rats
Schistosoma japonicum - metabolism
Secondary structure
Spectrometry, Fluorescence
Spectrophotometry
Spectroscopy, Fourier Transform Infrared
Temperature
Tertiary structure
Ultraviolet Rays
Ultraviolet spectra
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Summary:Domain 1 of the cell adhesion protein CD2 (CD2-1) has an all beta-structure typical of proteins belonging to the immunoglobin superfamily. It has a remarkable ability to fold as a native monomer or a metastable intertwined dimer. To understand the origin of structural rearrangements of CD2-1, we have studied equilibrium unfolding of the protein using various biophysical spectroscopic techniques. At temperatures above approx 68 degrees C, a partially folded state of CD2-1 (H state) with a distinct secondary structure, involving largely exposed aromatic and hydrophobic residues and a substantially perturbed tertiary structure, is observed. In contrast, an unfolded state (D state) of CD2-1 with random-coil-like secondary and tertiary structures is observed in 6 M GuHCl. This partially folded high-temperature state has increased negative molar ellipticity at 222 nm in far-ultraviolet CD spectra, implying formation of a non-native helical conformation. The existence of this non-native high-temperature intermediate is consistent with relatively high intrinsic helical propensities in the primary sequence of CD2-1. This conformational flexibility may be important in the observed domain swapping of CD2-1.
ISSN:1085-9195
1085-9195
1559-0283
DOI:10.1385/CBB:36:1:01