Search results
Results from the WOW.Com Content Network
Image of CD4 co-receptor binding to MHC (Major Histocompatibility Complex) non-polymorphic region. In molecular biology, CD4 (cluster of differentiation 4) is a glycoprotein that serves as a co-receptor for the T-cell receptor (TCR). CD4 is found on the surface of immune cells such as helper T cells, monocytes, macrophages, and dendritic cells.
CD4 immunoadhesin was first developed in the mid-1990s as a potential therapeutic agent and treatment for HIV/AIDS. The protein is a fusion of the extracellular domain of the CD4 receptor and the Fc domain of human immunoglobulin G (IgG), the most abundant antibody isotype in the human body. [1]
The CD4 receptor in particular interacts with murine MHC-II following the "ball-on-stick" model, where the Phe-43 ball fits into the conserved hydrophobic α2 and β2 domain residues. [5] During binding with MHC-II, CD4 maintains independent structure and does not form any bonds with the TCR receptor.
The extracellular and transmembrane part of the coreceptor is from wild-type CD8 coreceptor, whereas the intracellular domain from CD4 coreceptor. [1] This model was created to examine role of coreceptor coupling to Lck (lymphocyte-specific protein tyrosine kinase) [1] as the CD4 and CD8 coreceptors have an Lck-binding site in their ...
The motif contains a tyrosine separated from a leucine or isoleucine by any two other amino acids, giving the signature YxxL/I. [1] Two of these signatures are typically separated by between 6 and 8 amino acids in the cytoplasmic tail of the molecule (YxxL/Ix (6-8) YxxL/I). However, in various sources, this consensus sequence differs, mainly in ...
The binding of CD154 on T H cells to CD40 activates antigen presenting cells and induces a variety of downstream effects. Activated CD4+ T cells primarily exhibit its ligand CD40L/CD154 to antigen-presenting cells including dendritic cells (DCs), B cells, macrophages, classical and non-classical monocytes, on a variety of non-immune cells ...
SIRP β and γ have the similar extracellular structure but different cytoplasmic regions giving contrasting types of signals. SIRP α polymorphisms are found in ligand-binding IgSF V-set domain but it does not affect ligand binding. One idea is that the polymorphism is important to protect the receptor of pathogens binding. [6] [9]
SIP is an open source software tool used to connect computer programs or libraries written in C or C++ with the scripting language Python.It is an alternative to SWIG.. SIP was originally developed in 1998 for PyQt — the Python bindings for the Qt GUI toolkit — but is suitable for generating bindings for any C or C++ library.