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Mol. Cells 2004; 18(1): 24-29

Published online January 1, 1970

© The Korean Society for Molecular and Cellular Biology

Solution Structure of the Cytoplasmic Domain of Human CD99 Type I

Hai-Young Kim, Young Mee Kim, Young-Kee Shin, Seong-Hoe Park, Weontae Lee

Abstract

Human CD99, which is encoded by the mic2 gene, is a ubiquitous 32 kDa transmembrane protein. Its major cellular functions are related to homotypic cell adhesion, apoptosis, vesicular protein transport, and differentiation of thymocytes or T cells. Recent reports have suggested that expression of a splice variant of CD99 increases the invasiveness of human breast cancer cells. In order to determine the structural basis of CD99 function, we have initiated structural studies on the human CD99 Type I cytoplasmic domain (hCD99cytoI) using circular dichroism and multi-dimensional NMR spectroscopy. The solution structure of hCD99cytoI shows that it has a hairpin shape anchored by two flexible loops. Consequently, hCD99cytoI does not have any regular secondary structural element; however, the NMR and CD data indicate that it possesses an intrinsic helical nature.

Keywords Apoptosis; Circular Dichroism; hCD99cytoI; NMR Spec-troscopy

Article

Research Article

Mol. Cells 2004; 18(1): 24-29

Published online August 31, 2004

Copyright © The Korean Society for Molecular and Cellular Biology.

Solution Structure of the Cytoplasmic Domain of Human CD99 Type I

Hai-Young Kim, Young Mee Kim, Young-Kee Shin, Seong-Hoe Park, Weontae Lee

Abstract

Human CD99, which is encoded by the mic2 gene, is a ubiquitous 32 kDa transmembrane protein. Its major cellular functions are related to homotypic cell adhesion, apoptosis, vesicular protein transport, and differentiation of thymocytes or T cells. Recent reports have suggested that expression of a splice variant of CD99 increases the invasiveness of human breast cancer cells. In order to determine the structural basis of CD99 function, we have initiated structural studies on the human CD99 Type I cytoplasmic domain (hCD99cytoI) using circular dichroism and multi-dimensional NMR spectroscopy. The solution structure of hCD99cytoI shows that it has a hairpin shape anchored by two flexible loops. Consequently, hCD99cytoI does not have any regular secondary structural element; however, the NMR and CD data indicate that it possesses an intrinsic helical nature.

Keywords: Apoptosis, Circular Dichroism, hCD99cytoI, NMR Spec-troscopy

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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