| 词条 | TACI-CRD2 protein domain |
| 释义 |
| Symbol = TACI-CRD2 | Name = TACI-CRD2 | image = PDB 1xu1 EBI.jpg | width = | caption = the crystal structure of april bound to taci | Pfam = PF09305 | Pfam_clan = | InterPro = IPR015384 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, this protein domain, TACI-CRD2 represents the second cysteine-rich protein domain found in the TACI family of proteins. Members of this family are predominantly found in tumour necrosis factor receptor superfamily, member 13b (TACI), and are required for binding to the ligands APRIL and BAFF.[1] TACI-CRD2 stands for Transmembrane Activator and CAML Interactor- Cysteine Rich Domain 2. FunctionTACI functions as a negative regulator of BAFF function given that loss of TACI expression results in the overproduction of B lymphocytes, a type of white blood cell that guards against infection.Cytokines can be grouped into a family on the basis of sequence, functional and structural similarities.[2][3][4] Tumor necrosis factor (TNF) (also known as TNF-alpha or cachectin) is a cytotoxin which is derived from a form of white blood cell called monocytes. It is thought to cause tumour regression, septic shock and cachexia.[5][6] The protein is synthesised as a prohormone with an unusually long and atypical signal sequence, which is absent from the mature secreted cytokine.[7] A short hydrophobic stretch of amino acids serves to anchor the prohormone in lipid bilayers.[8] Both the mature protein and a partially processed form of the hormone are secreted after cleavage of the propeptide.[8]There are a number of different families of TNF, but all these cytokines seem to form homotrimeric (or heterotrimeric in the case of LT-alpha/beta) complexes that are recognised by their specific receptors. TACI is a member of the tumor necrosis factor receptor superfamily and has an important role as regulator of B cell function. TACI binds two ligands, APRIL and BAFF, which it binds to with high affinity and contains two cysteine-rich domains (CRDs) in its extracellular region. FormationTACI-CRD1 forms TACI-CRD2 by removing the N-terminal cysteine rich domain by alternative splicing. This shorter form is capable of ligand-induced cell signaling and that the second CRD alone (TACI-CRD2) contains full affinity for both ligands. LigandsThe ligands are type II transmembrane protein cytokines that have various effects on immune cells, including acting as a:
APRIL (also known as TNSF13A, TALL-2, and TRDL-1) is a TNF ligand that is overexpressed by some tumours. References1. ^{{cite journal | vauthors = Hymowitz SG, Patel DR, Wallweber HJ, Runyon S, Yan M, Yin J, Shriver SK, Gordon NC, Pan B, Skelton NJ, Kelley RF, Starovasnik MA | title = Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding | journal = J. Biol. Chem. | volume = 280 | issue = 8 | pages = 7218–27 |date=February 2005 | pmid = 15542592 | doi = 10.1074/jbc.M411714200 | url = }} {{InterPro content|IPR015384}}2. ^{{cite journal | vauthors = Peitsch MC, Jongeneel CV | title = A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors | journal = Int. Immunol. | volume = 5 | issue = 2 | pages = 233–8 |date=February 1993 | pmid = 8095800 | doi = 10.1093/intimm/5.2.233| url = }} 3. ^{{cite journal | vauthors = Farrah T, Smith CA | title = Emerging cytokine family | journal = Nature | volume = 358 | issue = 6381 | pages = 26 |date=July 1992 | pmid = 1377364 | doi = 10.1038/358026b0 | url = }} 4. ^{{cite journal | author = Bazan JF | title = Emerging families of cytokines and receptors | journal = Curr. Biol. | volume = 3 | issue = 9 | pages = 603–6 |date=September 1993 | pmid = 15335677 | doi = 10.1016/0960-9822(93)90009-D| url = }} 5. ^{{cite journal | vauthors = Fransen L, Müller R, Marmenout A, Tavernier J, Van der Heyden J, Kawashima E, Chollet A, Tizard R, Van Heuverswyn H, Van Vliet A | title = Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic expression | journal = Nucleic Acids Res. | volume = 13 | issue = 12 | pages = 4417–29 |date=June 1985 | pmid = 2989794 | pmc = 321797 | doi = 10.1093/nar/13.12.4417| url = }} 6. ^{{cite journal | vauthors = Kriegler M, Perez C, DeFay K, Albert I, Lu SD | title = A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF | journal = Cell | volume = 53 | issue = 1 | pages = 45–53 |date=April 1988 | pmid = 3349526 | doi = 10.1016/0092-8674(88)90486-2| url = }} 7. ^{{cite journal | vauthors = Sherry B, Jue DM, Zentella A, Cerami A | title = Characterization of high molecular weight glycosylated forms of murine tumor necrosis factor | journal = Biochem. Biophys. Res. Commun. | volume = 173 | issue = 3 | pages = 1072–8 |date=December 1990 | pmid = 2268312 | doi = 10.1016/S0006-291X(05)80895-2| url = }} 8. ^1 {{cite journal | vauthors = Cseh K, Beutler B | title = Alternative cleavage of the cachectin/tumor necrosis factor propeptide results in a larger, inactive form of secreted protein | journal = J. Biol. Chem. | volume = 264 | issue = 27 | pages = 16256–60 |date=September 1989 | pmid = 2777790 | doi = | url = }} 2 : Protein domains|Protein families |
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