Extracellular domain

Extracellular domain is part of the receptor so as to protrude from the outer membrane of the cell organelles and cells. If you have multiple intersecting bilayer, the polypeptide chains of the receptor may include a “line” of adherent plurality extracellular domain, a membrane. By definition, recognize, specific ligand, e.g., hormones or neurotransmitters (However, some receptors and respond to changes in membrane potential) This is because that corresponds to the basic functions of the receptors, many the receptors, these ligands bind to the extracellular domain.


The prediction of protein function from the array, you may be a difficult process fraught with pitfalls that are associated with divergence of the sequence, the function of the non-equivalent homologous to unequal multi-domain architecture. Being able to predict the conditions of cellular functions of the multi-domain proteins, especially the opening of the regulatory domain is important. However, it is preferred divergent homologs in sequence, it is possible also homologs among other organisms, will be held in common, these domains can occur in the context of a number of molecules. For example, family of protein kinase C isozymes in what can not be seen clearly in vertebrates and yeast still means that their condition is the same regulatory domain. To compound these problems, usually, a family of homologous domains, can be different in the maintenance of active site residues or key binding determinants, but has a variety of functions similar to another.

We have addressed these problems by providing a database and web-based tool that allows the identification of homologues domain users different sequences. Prediction of domain removes the misannotations sequence that occurs when comparing the pair multi-domain protein sequences and contrast the domain homologous architectures. This procedure, to facilitate to improve the signal-to-noise of demand by it, the subsequent consideration of sequence regions without annotation. The initial release of SMART databases that are focused on signaling proteins. They include a large variety of regulatory domains non-enzymatic, to mediate the transmission and regulation of extracellular signals to the nucleus.

It is a major health problem as antigenic variants of influenza virus. However, the influenza strains All extracellular domain of a protein that is a small virus code M2 ​​is flat. We fused the M2 domain first hepatitis B virus core (HBc antibody) proteins in order to create the code M2HBc fusion gene genetically expressed in E. coli efficiently this gene. Intranasal administration or intraperitoneal, purification M2HBc particles mice provides protection for 90-100% with respect to lethal challenge virus. Protection is mediated by a transfer from antibodies and serum. Enhanced immunogenicity of the extracellular domain of M2 in anti-HBc particles, allows extensive long-term protection against influenza virus infection.

Inhibitory neurotransmission is mediated by GABA mainly. Metabolism GABA (B) receptors are G protein-coupled receptor is a central brain function in mammals. Failure of GABA (B) receptors have been implicated in neurological diseases several. GBR1 GBR2 sub GBR1 is responsible for G-protein coupling in charge of GBR2 and ligand binding function as (B) receptor heterodimer assembly GABA. Here, it is shown to react foreign domain GBR1 are selective agonists directly GBR2 ectodomain, and increase the affinity of the agonist by stabilizing the conformation of the binding GBR1. We show the crystal structure of the extracellular domain GBR2 reveal the polarity interface heterodimer. In addition, I will identify the heterodimer of a specific contact of GBR1 residues of two subunits that are involved in ligand recognition. Finally, the data structural and functional we will mean asymmetry activated state GABA is specific to GABA operability system (B) receptor structure constant is open ectodomain GBR2 This suggests adopting the structure.

Changes in the regulatory target in the shape of epithelial cells cells that contribute to the organs and tissues of most, is the basis of morphogenesis. Crumbs (CRB) is a main determinant for controlling the apical epithelial apicobasal polarity. This provides evidence for a new role of stabilization to control the shape of the cells through the position of the adhesive bond with the apical domain organization and localization apex CRB. We believe that stability extracellular domain apex CRB is required. Vivo results suggest that mediates CRB-CRB interactions inner facing the extracellular domain support CRB apical cell membrane stability. By indicating in sufficient to promote cell aggregation in in vitro, the CRB extracellular domain confirmed the interaction CRB-CRB cells We further. Furthermore, it was reported that addition mediated CRB apical regulated by the extracellular domain is necessary in order to maintain the CRB top low polarity. Our results, and provides a new insight into the mechanism of cellular mechanisms of organizational structure and the top low polarity.