Angiotensin-Converting Enzyme: Difference between revisions
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===Structure of ACE1=== | ===Structure of ACE1=== | ||
The larger, somatic form of ACE1 has two metalloproteinase domains (N- and C-terminal domains), each containing the canonical Zn binding motif, HEXXH. Despite their similar structures and protease activity, only the C-terminal domain is critical for blood pressure regulation.<ref>PMID:11303049</ref> The smaller, testis-specific form of ACE1 (tACE) only contains the C-terminal metalloproteinase domain (identical to that of somatic ACE1), along with a hydrophobic membrane-anchoring domain and a small highly glycosylated N-terminal region. <ref name="Brew"/> The structure of tACE adopts a predominantly helical ellipsoid structure with a central groove extending 30 angstroms into the molecule, dividing the protein into two subdomains, S1 and SII. The boundaries of the groove are formed by helices 13, 14, 15, and 17 as well as beta strand 4. On top of the groove a lid is formed by helices 1, 2, and 3, preventing access of large polypeptides to the active-site cleft and adding to ACE1’s specificity. <ref name="Natesh">PMID:12540854</ref> | The larger, somatic form of ACE1 has two metalloproteinase domains (N- and C-terminal domains), each containing the canonical Zn binding motif, HEXXH. Despite their similar structures and protease activity, only the C-terminal domain is critical for blood pressure regulation.<ref>PMID:11303049</ref> The smaller, testis-specific form of ACE1 (tACE) only contains the C-terminal metalloproteinase domain (identical to that of somatic ACE1), along with a hydrophobic membrane-anchoring domain and a small highly glycosylated N-terminal region. <ref name="Brew"/> The structure of tACE adopts a predominantly helical ellipsoid structure with a <scene name='Angiotensin-Converting_Enzyme/Central_groove/2'>central groove extending 30 angstroms into the molecule</scene> , dividing the protein into two subdomains, S1 (Green) and SII (Purple). The boundaries of the groove are formed by helices 13, 14, 15, and 17 as well as beta strand 4. On top of the groove a lid is formed by helices 1, 2, and 3, preventing access of large polypeptides to the active-site cleft and adding to ACE1’s specificity. <ref name="Natesh">PMID:12540854</ref> | ||
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