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domain architectures of proteins with an sti1 domain  (InterPro Inc)
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InterPro Inc domain architectures of proteins with an sti1 domain
Comparison of <t>Sti1</t> domains and the Sgt2-C cons model. A , multiple sequence alignment of Sgt2-C with STI1 domains (DP1, DP2) from STI1/Hop homologs. Helices are shown based on the Sgt2-C cons model and the Sc Sti1-DP1/2 structures. Species for representative sequences are from S. cerevisiae ( Scer ), S. pombe ( Spom ), C. thermophilum ( Cthe ), C. savignyi ( Csav ), and H. sapiens ( Hsap ). B , Cα ribbon of Sc Sgt2-C cons color-ramped with large hydrophobic sidechains shown as gray sticks (sulfurs in yellow ). C , similar to B for the solution NMR structure of Sti1-DP2 526–582 (PDBID: 2LLW) . D , superposition of the Sgt2-C cons ( blue ) and Sti1-DP2 526–582 ( red ) drawn as cartoons.
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Comparison of Sti1 domains and the Sgt2-C cons model. A , multiple sequence alignment of Sgt2-C with STI1 domains (DP1, DP2) from STI1/Hop homologs. Helices are shown based on the Sgt2-C cons model and the Sc Sti1-DP1/2 structures. Species for representative sequences are from S. cerevisiae ( Scer ), S. pombe ( Spom ), C. thermophilum ( Cthe ), C. savignyi ( Csav ), and H. sapiens ( Hsap ). B , Cα ribbon of Sc Sgt2-C cons color-ramped with large hydrophobic sidechains shown as gray sticks (sulfurs in yellow ). C , similar to B for the solution NMR structure of Sti1-DP2 526–582 (PDBID: 2LLW) . D , superposition of the Sgt2-C cons ( blue ) and Sti1-DP2 526–582 ( red ) drawn as cartoons.

Journal: The Journal of Biological Chemistry

Article Title: Molecular basis of tail-anchored integral membrane protein recognition by the cochaperone Sgt2

doi: 10.1016/j.jbc.2021.100441

Figure Lengend Snippet: Comparison of Sti1 domains and the Sgt2-C cons model. A , multiple sequence alignment of Sgt2-C with STI1 domains (DP1, DP2) from STI1/Hop homologs. Helices are shown based on the Sgt2-C cons model and the Sc Sti1-DP1/2 structures. Species for representative sequences are from S. cerevisiae ( Scer ), S. pombe ( Spom ), C. thermophilum ( Cthe ), C. savignyi ( Csav ), and H. sapiens ( Hsap ). B , Cα ribbon of Sc Sgt2-C cons color-ramped with large hydrophobic sidechains shown as gray sticks (sulfurs in yellow ). C , similar to B for the solution NMR structure of Sti1-DP2 526–582 (PDBID: 2LLW) . D , superposition of the Sgt2-C cons ( blue ) and Sti1-DP2 526–582 ( red ) drawn as cartoons.

Article Snippet: A , the domain architectures of proteins with an STI1 domain were obtained initially from InterPro ( ) and then adjusted as discussed in the text.

Techniques: Comparison, Sequencing

Various domain structures of STI1 and other helical-hand-containing proteins. A , the domain architectures of proteins with an STI1 domain were obtained initially from InterPro and then adjusted as discussed in the text. Each domain within a protein is colored relative to the key. B , structural comparison of various hydrophobic-binding helical-hand protein complexes. For each figure only relevant domains are included. Upper row , color-ramped cartoon representation with bound helices in purple . Lower row , accessible surface of each protein colored by hydrophobicity again with docked helical clients in purple . In order, the predicted complex of ySgt2-C cons and Sc Sbh2-TMD, DP1 domain from yeast Sti1 with N terminus containing H0 in gray ( Sc Sti1-DP1)(PDBID: 2LLV), human calmodulin ( Hs CALM2) bound to a hydrophobic domain of calcineurin ( Hs PPP3CA) (PDBID: 2JZI), and M domain of SRP54 from Oryctolagus cuniculus ( Oc SRP54-M) and the signal sequence of human transferrin receptor ( Hs TR-TMD) (PDBID: 3JAJ).

Journal: The Journal of Biological Chemistry

Article Title: Molecular basis of tail-anchored integral membrane protein recognition by the cochaperone Sgt2

doi: 10.1016/j.jbc.2021.100441

Figure Lengend Snippet: Various domain structures of STI1 and other helical-hand-containing proteins. A , the domain architectures of proteins with an STI1 domain were obtained initially from InterPro and then adjusted as discussed in the text. Each domain within a protein is colored relative to the key. B , structural comparison of various hydrophobic-binding helical-hand protein complexes. For each figure only relevant domains are included. Upper row , color-ramped cartoon representation with bound helices in purple . Lower row , accessible surface of each protein colored by hydrophobicity again with docked helical clients in purple . In order, the predicted complex of ySgt2-C cons and Sc Sbh2-TMD, DP1 domain from yeast Sti1 with N terminus containing H0 in gray ( Sc Sti1-DP1)(PDBID: 2LLV), human calmodulin ( Hs CALM2) bound to a hydrophobic domain of calcineurin ( Hs PPP3CA) (PDBID: 2JZI), and M domain of SRP54 from Oryctolagus cuniculus ( Oc SRP54-M) and the signal sequence of human transferrin receptor ( Hs TR-TMD) (PDBID: 3JAJ).

Article Snippet: A , the domain architectures of proteins with an STI1 domain were obtained initially from InterPro ( ) and then adjusted as discussed in the text.

Techniques: Comparison, Binding Assay, Sequencing