Solution structure of the cytoplasmic domain of human CD99 type I.
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.
Kim
Hai-Young
HY
Department of Biochemistry and Protein Network Research Center, Yonsei University, Seoul 120-749, Korea.
Kim
Young Mee
YM
Shin
Young-Kee
YK
Park
Seong-Hoe
SH
Lee
Weontae
W
D000071443:12E7 Antigen; D000595:Amino Acid Sequence; D015703:Antigens, CD / Q000737:chemistry* / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
D000071443:12E7 Antigen; D015703:Antigens, CD; C061828:CD99 protein, human; D015815:Cell Adhesion Molecules