User:Letícia Oliveira Rojas Cruz/Sandbox 1
From Proteopedia
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The '''<scene name='10/1083732/Peptidase_domain/2'>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/2'>Subdomain I</scene> (residues 19–400) and <scene name='10/1083732/Subdominio_2_cterm/2'>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. | The '''<scene name='10/1083732/Peptidase_domain/2'>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/2'>Subdomain I</scene> (residues 19–400) and <scene name='10/1083732/Subdominio_2_cterm/2'>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. | ||
- | An important structure within the Subdomain II is the '''Ferredoxin-like fold''', also known as the neck domain, formed by residues approximately between 616 and 726. | ||
- | This region connects the Peptidase Domain to the Transmembrane Domain and is structurally characterized by four alpha helices and four beta sheets arranged in a compact and stable configuration, with a central beta-sheet flanked by alpha helices, contributing to the overall tertiary structure of ACE2. | ||
- | + | An important region following the Peptidase Domain is the '''<scene name='10/1083732/Collectrin-like_domain/3'>Collectrin-like Domain</scene>''' (CLD), also described structurally as a ferredoxin-like fold or neck domain, comprising residues approximately between 616 and 726. This domain connects the Peptidase Domain to the Transmembrane Domain and is composed of '''{{Font color|gold|4 beta sheets}}''' and '''{{Font color|deeppink|4 alpha-helices}}''', arranged around a hydrophobic core. Its fold, characterized by a central beta-sheet flanked by alpha helices, plays a crucial role in stabilizing ACE2 dimers, which will be detailed later on this page. | |
The <scene name='10/1083732/Transmembrane_domain/1'>Transmembrane Domain</scene> is composed of a '''{{Font color|red|single alpha helix}}''', made of a majority of <scene name='10/1083732/Transmembrane_domain_hydrop/1'>hydrophobic residues</scene> (in '''{{Font color|gray|gray}}'''). This characteristic allows ACE2 to be anchored in the plasma membrane, due to its hydrophobic nature. | The <scene name='10/1083732/Transmembrane_domain/1'>Transmembrane Domain</scene> is composed of a '''{{Font color|red|single alpha helix}}''', made of a majority of <scene name='10/1083732/Transmembrane_domain_hydrop/1'>hydrophobic residues</scene> (in '''{{Font color|gray|gray}}'''). This characteristic allows ACE2 to be anchored in the plasma membrane, due to its hydrophobic nature. |
Revision as of 20:17, 22 June 2025
Introduction
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