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> (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/2'>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|orchid|polar}}''' ones are towards the outside part of the molecule.
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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/2'>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|orchid|polar}}''' ones are towards the outside part of the molecule.
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The following domain is the '''<scene name='10/1083732/Collectrin-like_domain/3'>Collectrin-like Domain</scene>''', formed by '''{{Font color|gold|4 beta sheets}}''' and '''{{Font color|deeppink|3 alpha-helices}}''' that make a hydrofobic core, structure that is important for stabilizing ACE2 dimers, which will be represented later on this page.
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The Transmembrane Domain
== Function ==
== Function ==

Revision as of 15:13, 22 June 2025

Introduction

Caption for this structure

Drag the structure with the mouse to rotate

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

Proteopedia Page Contributors and Editors (what is this?)

Letícia Oliveira Rojas Cruz

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