Structure of Bovine CD46 Ectodomain

نویسندگان

چکیده

CD46, or membrane cofactor protein, is a type-one transmembrane protein from the complement regulatory family. Alongside its role in activation, CD46 involved many other processes, T-cell activation to reproduction. It also referred as pathogen magnet, because it used receptor by multiple bacteria and viruses. Bovine (bovCD46) particular bovine viral diarrhoea virus entry, an economically important disease cattle industries. This study presents X-ray crystallographic structure of extracellular region bovCD46, revealing four-short-consensus-repeat (SCR) similar that human CD46. SCR1-3 are arranged linearly, while SCR 4 has reduced interface angle, resulting hockey stick-like appearance. The reveals interaction site SCR1, which likely confer pestivirus specificity for their target host, Insights gained structural information on receptors, such could offer valuable guidance future control strategies.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

CD46 is a cellular receptor for bovine viral diarrhea virus.

Various monoclonal antibodies (MAbs) that recognize cell surface proteins on bovine cells were previously shown to efficiently block infection with bovine viral diarrhea virus (BVDV) (C. Schelp, I. Greiser-Wilke, G. Wolf, M. Beer, V. Moennig, and B. Liess, Arch. Virol. 140:1997-2009, 1995). With one of these MAbs, a 50- to 58-kDa protein was purified from calf thymus by immunoaffinity chromatog...

متن کامل

Comparative fluorescence analysis of the bovine sperm using IVA-520 (anti-CD46 antibody) and lectins: probable localisation of CD46 on bovine sperm membrane.

Membrane cofactor protein (CD46) is complement regulatory protein with probable function in the reproduction process. Expression of CD46 on human, mice, rat and guinea pig spermatozoa is restricted to the inner acrosomal membrane. In spite of the presence of anti-sperm antibodies and other potential complement activating agents in follicular fluid, CD46 is not expressed on the plasma membrane o...

متن کامل

Crystal structure of the ectodomain of human transferrin receptor.

The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome. The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit. One domain closely...

متن کامل

Structure of the Plexin Ectodomain Bound by Semaphorin-Mimicking Antibodies

Semaphorin family proteins act on cells to mediate both repulsive and attractive guidance via binding to plexin family receptors, thereby playing fundamental roles in the morphogenesis and homeostasis of various tissues. Although semaphorin-plexin signaling is implicated in various diseases and is thus a target of intensive research, our mechanistic understanding of how semaphorins activate ple...

متن کامل

Dependence of purinergic P2X receptor activity on ectodomain structure.

Purinergic receptors (P2XRs) activate and desensitize in response to the binding of extracellular nucleotides in a receptor- and ligand-specific manner, but the structural bases of their ligand preferences and channel kinetics have been incompletely characterized. Here we tested the hypothesis that affinity of agonists for binding domain accounts for a ligand-specific desensitization pattern. W...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Viruses

سال: 2023

ISSN: ['1999-4915']

DOI: https://doi.org/10.3390/v15071424