Receptor-binding regions

Extensive mutagenesis studies have provided information related to the structural integrity, receptor binding region, and residues that are important for IL-1 function. Site-directed mutagenesis (SDM) can create a single-site mutant and its receptor binding and bioactivity values can be calculated. The results... 

The LDL particles contain one apoB-100 as the structural protein and are the major cholesterol-transporting lipoproteins in human blood. Clearance of LDL from blood is mediated by the interaction of apoB-100 with the LDLR. Genetic defects either in the receptor binding region of apoB-100 or in the LDLR lead to decreased clearance of LDL and hence to their accumulation in the blood. The major metabolic pathways of the lipoprotein metabolism are shown in Fig. 5.2.1. 

Martin, E. L., Rens-Domiano, S., Schatz, P.J., and Hamm, H. E. (1996). Potent peptide analogues of a G protein receptor-binding region obtained with a combinatorial library. / Biol. Chem. 271, 361-366. 

Fig. 4. Specificity determined by availability of receptor binding regions of DNA. With an oestrogen (E) sensitive gene, the receptor complex binds to specific regions of DNA (steroid response element) which influences the efficiency of mRNA initiation. If the response element is blocked, the gene is unresponsive to the steroid.

These studies were important in that they represented the first antibody-virus complexes of an enveloped virus, helped identify the location of the receptor-binding region of this family of viruses, and were another example of using antibodies to elucidate viral topography. 

These studies have all shown the importance of hybrid technology. Antibodies have been used to elucidate the architecture of viruses and to identify receptor-binding regions. They have directly addressed the mechanism of antibody-mediated neutralization, which has greatly impacted the development of vaccines. Finally, they have improved our understanding about the forces that have driven the evolution of viral structure. It is likely that such studies will continue to help us understand the architecture of macro-macromolecular complexes and the dynamics of these viral capsids. 

Bhat S, Mettus R, Reddy E, Ugen K, Srikanthan V, Williams W, Weiner D. The galactosyl ceramide/snlfatide receptor binding region of HIV-lgpl20 maps to amino acids 206-275. Aids Res. Hum. Retrovirus. 1993 9 175-181. 

Muscarinic Cholinergic Receptor Binding Regional Distribution In Monkey Brain. Brain Res. 66 541 546. 

Muscarinic cholinergic receptor binding regional distribution in monkey brain Brain Res. 66, 541-546 ... 

In terms of the present discussion of the receptor-binding region of apoE, the effect of the loss of Arg-158 on receptor interaction was consistent with the chemical modification studies (Mahley et al., 1977a Weisgraber et al, 1978) and with the fact that Arg-158 was within the basic region of apoE noted above. 

Fig. 14. Ribbon model of the structure of the 22-kDa fragment of human apoli-poprolein E3. Four of the five helices (helices 1-4) are arranged in an antiparallel four-helix bundle. The four-helix bundle can be viewed as a rectangle, with approximate dimensions of 20 x 20 x 65 A. The receptor-binding region of apoE (—residues 130-150) is indicated on helix 4. The residue numbers at the start and end of each helix are indicated.

As discussed in Section III,D, several lines of evidence indicate that Arg-158 does not interact directly with the LDL receptor, but that this residue has an indirect effect on the receptor-binding region (residues... 

The H chains are less conserved than the L chains and the carboxyl-terminal part of the H chain (He) is the most variable region of the toxin (Fig. 2) (Minton, 1995). This is consistent with the notions that the He domain is involved in binding to the nerve terminals and that different neurotoxins bind to different cognate receptors. On this basis it may be suggested that the receptor binding regions of TeTx and BoNTs are mainly located within the 180 carboxy-terminal residues of the H chain. 

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