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Synthetic peptides as structural maquettes of Angiotensin-I converting enzyme catalytic sites.

Spyranti Z, Galanis AS, Pairas G, Spyroulias GA, Manessi-Zoupa E, Cordopatis P - Bioinorg Chem Appl (2010)

Bottom Line: The rational design of synthetic peptides is proposed as an efficient strategy for the structural investigation of crucial protein domains difficult to be produced.Only after half a century since the function of ACE was first reported, was its crystal structure solved.Structural investigations of the synthetic peptides, representing the two different somatic isoform active sites, through circular dichroism and NMR experiments are reported.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmacy, University of Patras, GR-26504, Patras, Greece.

ABSTRACT
The rational design of synthetic peptides is proposed as an efficient strategy for the structural investigation of crucial protein domains difficult to be produced. Only after half a century since the function of ACE was first reported, was its crystal structure solved. The main obstacle to be overcome for the determination of the high resolution structure was the crystallization of the highly hydrophobic transmembrane domain. Following our previous work, synthetic peptides and Zinc(II) metal ions are used to build structural maquettes of the two Zn-catalytic active sites of the ACE somatic isoform. Structural investigations of the synthetic peptides, representing the two different somatic isoform active sites, through circular dichroism and NMR experiments are reported.

No MeSH data available.


(a) Ensemble of DYANA 30 best models of the Zn2+-ACEC(37) (corresponds to His958- Ala994of the human somatic form), calculated with NMR data. (b) Ribbon diagram of Zn2+-ACEC(37) peptide.
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fig7: (a) Ensemble of DYANA 30 best models of the Zn2+-ACEC(37) (corresponds to His958- Ala994of the human somatic form), calculated with NMR data. (b) Ribbon diagram of Zn2+-ACEC(37) peptide.

Mentions: The Zn2+-ACEC(37) backbone is characterized by the high content of helical structure. Two helical conformations were observed at both N- and C-termini, spanning residues His6–Lys14 and Phe28–Val35, respectively. Moreover, a 310- helix comprised of a 5-residue segment (Ala19-Gly23) has been identified for the intermediate fragment. In accordance with the Zn2+-ACEN(37) peptide, the two zinc-binding motifs of Zn2+-ACEC(37) are in spatial proximity as manifested by long-range NOEs, such as those between His6/Ile7 and His29 as well as Gln8/Gln12 with Ala19 (Figure 7).


Synthetic peptides as structural maquettes of Angiotensin-I converting enzyme catalytic sites.

Spyranti Z, Galanis AS, Pairas G, Spyroulias GA, Manessi-Zoupa E, Cordopatis P - Bioinorg Chem Appl (2010)

(a) Ensemble of DYANA 30 best models of the Zn2+-ACEC(37) (corresponds to His958- Ala994of the human somatic form), calculated with NMR data. (b) Ribbon diagram of Zn2+-ACEC(37) peptide.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2902127&req=5

fig7: (a) Ensemble of DYANA 30 best models of the Zn2+-ACEC(37) (corresponds to His958- Ala994of the human somatic form), calculated with NMR data. (b) Ribbon diagram of Zn2+-ACEC(37) peptide.
Mentions: The Zn2+-ACEC(37) backbone is characterized by the high content of helical structure. Two helical conformations were observed at both N- and C-termini, spanning residues His6–Lys14 and Phe28–Val35, respectively. Moreover, a 310- helix comprised of a 5-residue segment (Ala19-Gly23) has been identified for the intermediate fragment. In accordance with the Zn2+-ACEN(37) peptide, the two zinc-binding motifs of Zn2+-ACEC(37) are in spatial proximity as manifested by long-range NOEs, such as those between His6/Ile7 and His29 as well as Gln8/Gln12 with Ala19 (Figure 7).

Bottom Line: The rational design of synthetic peptides is proposed as an efficient strategy for the structural investigation of crucial protein domains difficult to be produced.Only after half a century since the function of ACE was first reported, was its crystal structure solved.Structural investigations of the synthetic peptides, representing the two different somatic isoform active sites, through circular dichroism and NMR experiments are reported.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmacy, University of Patras, GR-26504, Patras, Greece.

ABSTRACT
The rational design of synthetic peptides is proposed as an efficient strategy for the structural investigation of crucial protein domains difficult to be produced. Only after half a century since the function of ACE was first reported, was its crystal structure solved. The main obstacle to be overcome for the determination of the high resolution structure was the crystallization of the highly hydrophobic transmembrane domain. Following our previous work, synthetic peptides and Zinc(II) metal ions are used to build structural maquettes of the two Zn-catalytic active sites of the ACE somatic isoform. Structural investigations of the synthetic peptides, representing the two different somatic isoform active sites, through circular dichroism and NMR experiments are reported.

No MeSH data available.