LitCovid-sentences  

PMC:7556165 / 7787-10683 JSONTXT 16 Projects

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Id Subject Object Predicate Lexical cue
T54 0-17 Sentence denotes Structure of ACE2
T55 18-139 Sentence denotes ACE2 is a 40 kb gene and it is positioned on chromosome Xp22, differently from ACE gene that is located on chromosome 17.
T56 140-197 Sentence denotes The 18 exons of ACE2 are remarkably similar to ACE exons.
T57 198-487 Sentence denotes The ACE2 gene depicts a large polymorphism and several novel polymorphisms of ACE2, with specific geographical distribution, have been described and associated with susceptibility to hypertension and cardiovascular disease (Burrell et al., 2013; Patel et al., 2014; Pinheiro et al., 2019).
T58 488-608 Sentence denotes The ACE2 gene codifies for a typical zinc-metallopeptidase of 805 amino acids (120 kDa), with a unique catalytic domain.
T59 609-719 Sentence denotes Despite the high resemblance of ACE and ACE2, considerable differences exist in their substrates and products.
T60 720-809 Sentence denotes While ACE acts as dipeptidase, ACE2 removes only a single amino acid from its substrates.
T61 810-1061 Sentence denotes Therefore, ACE2 is not active in transforming angiotensin I to angiotensin II and in inactivating bradykinin; moreover, ACE2 is insensitive to ACE inhibitors, like lisinopril and captopril (Tipnis et al., 2000; Rice et al., 2004; Turner et al., 2004).
T62 1062-1159 Sentence denotes These differences depend on variances in the three-dimensional structure (3D) of the two enzymes.
T63 1160-1268 Sentence denotes Comparative homology modeling and crystallography contributed to shed light on ACE2 3D structure (Figure 1).
T64 1269-1421 Sentence denotes Prabakaran et al. (2004) clarified the major characteristic of ACE2, which is a deep channel on the summit of the protein, hosting the catalytic domain.
T65 1422-1570 Sentence denotes Specific loops, like the long loop N210-Q221 that is exclusive of ACE2, α helices and a portion of β-sheet are located around the catalytic channel.
T66 1571-1731 Sentence denotes The negative charge of the channel and the presence of distinct hydrophobic regions contribute to the specificity of the binding site (Prabakaran et al., 2004).
T67 1732-1994 Sentence denotes The determination of the crystal structure of the extracellular domain to 2.2-3-A resolution from Towler et al. (2004) and the model from Guy et al. (2003) showed that the catalytic domain of ACE and ACE2 are very conserved and have similar mechanisms of action.
T68 1995-2266 Sentence denotes The main difference stems from the smaller ACE2 pocket, thereby lodging only a single amino acid: the crucial substitution of the Gln281 in ACE binding pocket with Arg273 in ACE2 is likely to be responsible for the steric conflict (Guy et al., 2003; Towler et al., 2004).
T69 2267-2503 Sentence denotes Another surprise of the ACE2 structure was its C-terminal domain, which—differently from ACE—revealed high homology with collectrin, a renal protein, which is involved in amino acids trafficking through the membrane (Yang et al., 2017).
T70 2504-2540 Sentence denotes FIGURE 1 Crystal structure of ACE2.
T71 2541-2656 Sentence denotes The peptidase domain (PD) is in green, whereas the collectrin homology domain is enclosed in the light cyan square.
T72 2657-2802 Sentence denotes The active zinc ion is showed enclosed in a red circle, whereas the glycosylation moieties are showed as cyan cubes and denoted by dashed arrows.
T73 2803-2896 Sentence denotes The structures have been drawn from PDB 1R42 (Towler et al., 2004) by Mol on the PDB website.