Zinc-binding site

Figure 13.23 The F-G loop in the C-terminal domain of the prolactin receptor is involved in a unique interaction, (a) The F-G loop of the growth hormone receptor (blue) is not involved in any specific interactions with the growth hormone (red), (b) The F-G loop in the prolactin receptor forms a strong zinc-binding site that links the receptor (green) to the hormone (red). (Adapted from W. Somers et at.. Nature 372 478-481, 1994.)...

Carbonic anhydrase an insight into the zinc binding site and into the active cavity through metal substitution. I. Bertini, C. Luchinat and A. Scozzafava, Struct. Bonding (Berlin), 1982, 48, 46-92 (296). 

Bertini I, Luchinat C, Scozzafava A (1982) Carbonic Anhydrase An Insight into the Zinc Binding Site and into the Active Cavity Through Metal Substitution. 48 45-91 Bertrand P (1991) Application of Electron Transfer Theories to Biological Systems. 75 1-48 Bill E, see Trautwein AX (1991) 78 1-96 Bino A, see Ardon M (1987) 65 1-28 Blanchard M, see Linares C (1977) 33 179-207 Blasse G, see Powell RC (1980) 42 43-96... 

Bertini, /., Luchinat, C., Scozzafava, A. Carbonic Anhydrase An Insight into the Zinc Binding Site and into the Active Cavity Through Metal Substitution. Vol. 48, pp. 45-91. 

J.S. Valentine, M.W. Pantoliano, PJ. Mcdonnell, A.R. Burger, and S.J. Lippard, pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 76, 4245-4249 (1979). 

M.W. Pantoliano, P.J. McDonnell, and J.S. Valentine, Reversible loss of metal ions from the zinc binding site of copper-zinc superoxide dismutase. The low pH transition. J. Amer. Chem. Soc. 101, 6454— 6456 (1979). 

Jensen, A. A., Sheppard, P. 0., Jensen, L. B., O Hara, P. J., and Brauner-Osbome, H. (2001) Construction of a high affinity zinc binding site in the metabotropic glutamate receptor mGluRl. Noncompetitive antagonism from the amino-terminal domain of a family C G protein-coupled receptor. J. Biol. Chem. 276,10110-10118. 

Alberts, I. L., Nadassy, K., and Wodak, S. J. (1998) Analysis of zinc binding sites in protein crystal structures. Protein. Sci. 7,1700-1716. 

Norregaard, L., Frederiksen, D., Nielsen, E. O., and Gether, U. (1998) Delineation of an endogenous zinc-binding site in the human dopamine transporter. Embo. J. 17,4266 1273. 

Ippolito, J. A., Baird, T. T., Jr., McGee, S. A., Christianson, D. W., and Fierke, C. A. (1995) Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity. Proc. 

Figure 12.1 Zinc-binding sites in enzymes can be catalytic, structural or cocatalytic. The protein ligands are indicated by smaller filled circles. (From Auld, 2001. With kind permission of Springer Science and Business Media.)...

Papageorgiou, A.C., Acharya, K.R., Shapiro, R., Passalacqua, E.F., Brehm, R.D. and Tranter, H.S., Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site. Structure, 3, 769-779, 1995. 

Independently, Ruan etal. (1990) demonstrated that unnatural metal-ligating residues may likewise be utilized toward the stabilization of short a helices by transition metal ions (including Zn " ")—these investigators reported that an 11-mer is converted from the random coil conformation to about 80% a helix by the addition of Cd at 4°C. These results suggest that the engineering of zinc-binding sites in small peptides or large proteins may be a powerful approach toward the stabilization of protein secondary structure. 

The engineering of zinc-binding sites in a-helical peptides, where metal binding stabilizes protein tertiary structure, has been reported by Handel and DeGrado (1990). In these experiments zinc-binding sites are incorporated into a dimeric helix-loop—helix peptide (H3 2) and a protein composed of four helices connected by three short loop sequences (H3 4). a model of one subunit of the H3 2 dimer is found in Fig. 47. In addition to metal complexation by two histidine residues at positions n and n+4 of one a helix, the metal is coordinated by a third histidine residue of an adjacent a helix. The composition of the zinc coordination polyhedron is like that of carbonic anhydrase (i.e., Hiss), and spectroscopic results suggest that all three histidine residues are involved in zinc complexation. This work sets an important foundation... 

The zinc-binding site of carbonic anhydrase serves as a structural paradigm for the incorporation of a de novo zinc-binding site in an antibody (Iverson a/., 1990 Roberts cf a/., 1990 Tainer and Roberts, 1990). Because individual antibody light- and heavy-chain libraries can be com-... 

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