User:Letícia Oliveira Rojas Cruz/Sandbox 1

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The ACE2 protein gene has 40 kb and 18 exons. Its protein has 805 amino acids with a molecular weight of 120 kDa. Here, we have a view of the <scene name='10/1083732/Ace2_completa/2'>full ACE2 protein</scene>. It can be divided into 4 portions: Peptidase Domain (Residues 19–615), Collectrin-like Domain (Residues 616–740), Transmembrane Domain (Residues 741–761) and Intracellular C-terminal Tail (Residues 762–805), from '''{{Font color|blue|N-terminal}}''' to '''{{Font color|red|C-terminal}}'''.
The ACE2 protein gene has 40 kb and 18 exons. Its protein has 805 amino acids with a molecular weight of 120 kDa. Here, we have a view of the <scene name='10/1083732/Ace2_completa/2'>full ACE2 protein</scene>. It can be divided into 4 portions: Peptidase Domain (Residues 19–615), Collectrin-like Domain (Residues 616–740), Transmembrane Domain (Residues 741–761) and Intracellular C-terminal Tail (Residues 762–805), from '''{{Font color|blue|N-terminal}}''' to '''{{Font color|red|C-terminal}}'''.
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The <scene name='10/1083732/Peptidase_domain/1'>Peptidase Domain</scene> is responsible for the enzymatic activity of ACE2. This domain can be divided in two subdomains: <scene name='10/1083732/Subdominio_1_nterm/1'>Subdomain I</scene> and <scene name='10/1083732/Subdominio_2_cterm/1'>Subdomain II</scene>. Together, they form a substrate-binding cleft, where is located the '''<scene name='10/1083732/Sitio_zinco_com_residuos/1'>catalytic site</scene>'''. Within this site, a '''{{Font color|lime|zinc-ion}}''' is associated with the residues '''His374''', '''His378''', and '''Glu402''', which are going to perform a nucleophilic attack on the peptide bond of the substrate, leading to its cleavage.
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The <scene name='10/1083732/Peptidase_domain/1'>Peptidase Domain</scene> is responsible for the enzymatic activity of ACE2. This domain can be divided in two subdomains: <scene name='10/1083732/Subdominio_1_nterm/1'>Subdomain I</scene> (residues 19–400) and <scene name='10/1083732/Subdominio_2_cterm/1'>Subdomain II</scene> (residues 401–615). Together, they form a substrate-binding cleft, where is located the '''<scene name='10/1083732/Sitio_zinco_com_residuos/1'>catalytic site</scene>''', denominated '''HEXXH+E zinc-binding motif'''. Within this site, a '''{{Font color|lime|zinc-ion}}''' is associated with the residues '''His374''', '''His378''', and '''Glu402''', which are going to perform a nucleophilic attack on the peptide bond of the substrate, leading to its cleavage. '''<scene name='10/1083732/Peptidase_domain_hydrofobic/1'>Hydrophobic portions</scene>''' within each subdomain, composed mainly of nonpolar residues provide tertiary structural stability, maintaining the correct spatial arrangement of catalytic residues. In the animation, we can observe a concentration of the '''{{Font color|gray|hydrophobic residues}}''' towards the center of the molecule, while the '''{{Font color|purple|polar}}''' ones are towards the outside part of the molecule.
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Revision as of 14:34, 22 June 2025

Introduction

Caption for this structure

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  3. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024

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Letícia Oliveira Rojas Cruz

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