Receptor binding domain

Manttari M, Koskinen P, Ehnholm C, Huttunen JK, Manninen V. Apolipo-protein E polymorphism influences the serum cholesterol response to dietary intervene blood is diminished due to mutations within the apoB-100 receptor binding domain [51]. A number of point mutations of the putativd its relation to E polymorphism. Orv Hetil 1994 135 735-741. 

T4-fiber fold Triple /i-helix Collar domain Receptor-binding domain... 

Fig. 6. Structure of the T4 short tail fiber. The structure of residues 246-527 is shown it is a composite of two partial structures (Thomassen et al., 2003 van Raaij et al., 2001a). The different domains are indicated the T4-fiber fold consisting of residues 246-286, the triple / -helix (residues 290-329), the collar domain (residues 330-396 and 518-527), and the receptor-binding domain (amino acids 397-517). The zinc ion in the center of the receptor-binding domain is shown as a gray sphere.

Guardado Calvo, P., Fox, G. C., Hermo Parrado, X. L., Llamas-Saiz, A. L., Costas, C., Martinez-Costas, J., Benavente, J., and van Raaij, M. J. (2005). Structure of the carboxy-terminal receptor-binding domain of avian reovirus fibre sigmaC. / Mol. Biol. 354, 137-149. 

Thomassen, E., Gielen, G., Schutz, M., Schoehn, G., Abrahams, J. P., Miller, S., and van Raaij, M. J. (2003). The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. J. Mol. Biol. 331, 361-373. 

Xia, D., Henry, L.J., Gerard, R. D., and Deisenhofer, J. (1994). Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution. Structure 2, 1259-1270. 

Many natural protein hgands bind to their receptors via interactions of a specific area of the protein backbone. The receptor binding domain of such a protein can be transferred into another protein, for instance a therapeutically active one. This technique is commonly applied in the preparation of recombinant targeting constructs, and will be discussed in Section 11.8.2. 

When the receptor binding domain is encoded in a small peptide sequence, the peptide hg-and can also be synthesized and conjugated chemically to the carrier protein. This approach was followed in our laboratory by Beljaars et al. for the development of carriers aimed at the hepatic stellate cell, a cell type involved in liver fibrosis [33] (see also Chapter 4). A peptide sequence derived from the receptor binding domains of collagen VI was incorporated into a cyclic peptide homing device, and subsequently conjugated to lysine residues of HSA. This carrier bound selectively to activated hepatic stellate cells and rapidly accumulated in the livers of fibrotic rats. 

Cytotoxins Cytokine, interleukin, growth factor or the receptor binding domains of these proteins Toxin, toxic protein or apoptosis-inducing protein IL-2-DAB TGFa-PE40 IL-2-BAX bFGF-SAP bFGF-RNase [123] [124,125] [126] [127] [128]... 

Fig. 9. RNA editing, (a) Unedited apolipoprotein B mRNA is translated to yield ApoB-100, a 4536-amino acid long polypeptide with structural domains for lipoprotein assembly and receptor binding functions (b) translation of the edited mRNA yields the shorter ApoB-48 which lacks the receptor binding domain.

Schmiedeberg N, Schmitt M, Rolz C, Truffault V, Sukopp M, Burgle M, et al. Synthesis, solution structure, and biological evaluation of urokinase type plasminogen activator (uPA)-derived receptor binding domain mimetics. J Med Chem 2002 45(23) 4984 1994. 

Fig. 2. Structures of the extracellular domains of Ephs and ephrins. The molecular surfaces (semi-transparent) are also indicated. (A) Structure of the ligand-binding domain of EphB2. The N- and C-termini of the molecule are labeled, as are the class-specificity loop (H-I) and the ligand-binding loops that are largely disordered in the absence of bound ephrin. (B) Structure of the extracellular receptor-binding domain of ephrin-B2. Indicated is the location of the receptor-binding G-H loop. (C) Structure of the EphB2/ephrin-B2 tetramer. Eph receptors are blue and ephrins are green. The high-affinity dimerization interfaces are indicated by arrows. (See Color Insert.)...

The ephrins possess a unique N-terminal receptor-binding domain (RBD) (Fig. 1), which is separated from the membrane via a linker of approximately forty amino acids. A-ephrins are attached to the cell via a GPl linkage. B-type ephrins have a transmembrane region and short but conserved 80-amino-acid cytoplasmic domain, which harbors a C-terminal PDZ-binding motif. 

M3 has two domains an N-terminal domain and a G-terminal domain, each composed of elaborated / -sandwiches with closest structural homologies to the G-terminal receptor binding domain of diptheria toxin, and the V-type Ig-fold, respectively. It exits in solution as a head to tail dimer, which leads to the formation of a cleft between the N-terminal domain of one subunit and the G-terminal domain of the other. Ghemokines bind within each cleft, thus forming a 2 2 complex. Figure lOA shows a surface... 

Apo-B-48 Chylomicrons Exclusively found in chylomicrons, derived from apo-B-100 gene by RNA editing in intestinal epithelium lacks the LDL receptor-binding domain of apo-B-100... 

Fig. 5 AD2 APOE structure and single nucleotide polymorphisms (SNPs). The general protein structure of apoE is shown (panel a). The two SNPs and corresponding protein locations are shown (rs429358 and rs7412 Cl 12R and R158C). The APOE i2, 3, (4 haplotype is shown in panel b. Receptor binding domain R. Scale is approximate...

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