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| Content Provider | Springer Nature Link |
|---|---|
| Author | Yang, Jenny J. Carroll, Amy R. Yang, Wei Ye, Yiming Nguyen, Christina N. |
| Copyright Year | 2000 |
| Abstract | Cell adhesion molecule, CD2, from the immunoglobulin superfamily, is comprised of antibodies and Ig-like domains and plays a fundamental role, not only in the immune system, but also in the interactions between cells, specifically in cell-cell adhesion. This study examines the N-terminal domain 1 of CD2 (CD2-1) at different pHs, and in 2,2,2-trifluoroethanol (TFE), using nears- and far-UV circular dichroism (CD), fluorescence, and $^{1}$H nuclear magnetic resonance to elucidate factors contributing to the Ig β-structure. Contrary to the complete unfolding induced by guanidinehydrochloride, CD2-1 retains its native tertiary structure at pHs from 1.0 to 10.0. Like the effects of high temperatures that have previously been observed, TFE reduces the integrity of the tertiary structure, while reorganizing the secondary structure from a native all-β-sheet to a significantly α-helical conformation. The induced helicity of CD2-1 correlates with the helicity inherent in its primary sequence. Our results suggest that electrostatic interactions are less important for the formation of the native secondary and tertiary structure of CD2-1, although they are crucial for CD2’s adhesion function. Interference with the protein’s hydrophobic interactions and hydrogen-bonding networks, however, causes significant changes in its conformation. Residues of CD2-1, with high conformational flexibility, may contribute for the formation of a metastable dimer by domain-swapping. |
| Starting Page | 253 |
| Ending Page | 273 |
| Page Count | 21 |
| File Format | |
| ISSN | 10859195 |
| Journal | Cell Biochemistry and Biophysics |
| Volume Number | 33 |
| Issue Number | 3 |
| e-ISSN | 15590283 |
| Language | English |
| Publisher | Humana Press |
| Publisher Date | 2000-01-01 |
| Publisher Place | Totowa |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Biochemistry Pharmacology/Toxicology Biotechnology Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine Biochemistry Biophysics |
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