İmmünoreseptör Tirozin Bazlı MotiflerÜzerine Bir Çalışma


Turhan K., Özdemir S., Zihni N. B., Kalaycı M. E., Ünsal S.

14. Tıp Bilişimi Kongresi, İzmir, Türkiye, 16 - 18 Mart 2023, ss.124-127

  • Yayın Türü: Bildiri / Özet Bildiri
  • Basıldığı Şehir: İzmir
  • Basıldığı Ülke: Türkiye
  • Sayfa Sayıları: ss.124-127
  • Karadeniz Teknik Üniversitesi Adresli: Evet

Özet

The cytoplasmic tyrosine structure patterns presented on immune receptor signaling proteins that activate, inhibit, and stimulate the immune system in depending on the cell type and particular conditions come in three different forms[1]. The immunoreceptor tyrosine-based inhibition motif (ITIM) has been identified in the intracytoplasmic domain of FcgRIIB and shows wide tissue distribution. ITIMs are the consensus sequence I/V/LxYxxL/V (V:Valine, Y:Tyrosine) with a tyrosine followed by a hydrophobic residue (I, V, or L) at the Y+3 position, followed by a less conserved hydrophobic residue at the Y-2 position (L: Leucine, I: Isoleucine, x: Any amino acid). The immunoreceptor tyrosine-based activation motif (ITAM) is found in multisubunit T-cell receptors (TCRs), B-cell receptors (BCRs), and Fc receptors (FcRs) [2]. ITAMs contain 2 copies of the YxxL/I sequence with six to eight residues among them [3]. The immunoreceptor tyrosine-based switch motif (ITSM) has been identified in the intracellular domain of the CD150 receptor, TxYxxL/V (T: Threonine). In most receptors, ITIMs and ITSMs are repeated after a weakly conserved sequence of about 15 to 30 amino acids between motifs [4]. Also, It is known that some viruses contain ITAM motifs, which are of great importance in intracellular signaling [5]. In this study, 3 motifs were screened on the human proteome. First of all, studies should be conducted on candidate proteins that may affect the signalization in the immune system for immune system-restricted motifs. The study is expected to be instructive in generating datasets in classification-based approaches, especially in personalized cancer immunotherapy.