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Structural differences in TRIM11 and TRIM36 PRYSPRY domains. (A) Asymmetric unit of the TRIM11 PRYSPRY structure showing subdomain swapping. β-strands 7 and 8 of chain A (shown in dark red) complete the canonical PRYSPRY fold in chain B (shown in gray), whereas the equivalent structural elements of chain B are disordered. (B) Symmetrical dimer in the crystal structure of the TRIM36 PRYSPRY domain. The dimer interface is formed via the insertion connecting the canonical β-strands 2 and 3. (C) Size-exclusion chromatography of the TRIM11 and TRIM36 PRYSPRY domain on a Superdex-75 column compared with the elution profiles of marker proteins. TRIM11 eluted at a retention time corresponding to a monomer (orange trace; theoretical MW of the monomer = 20.9 kDa), whereas TRIM36 eluted at a retention time corresponding to a dimer, in agreement with the structural data (magenta trace; theoretical MW of the dimer = 52.4 kDa). Marker proteins used: bovine serum albumin (MW = 66 kDa; Sigma-Aldrich), hen egg white ovalbumin (MW = 44 kDa, Sigma-Aldrich), bovine <t>erythrocyte</t> carbonic <t>anhydrase</t> (MW = 30 kDa, MP Biomedicals), bovine ribonuclease A (MW = 13.7 kDa, Sigma-Aldrich).
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Structural differences in TRIM11 and TRIM36 PRYSPRY domains. (A) Asymmetric unit of the TRIM11 PRYSPRY structure showing subdomain swapping. β-strands 7 and 8 of chain A (shown in dark red) complete the canonical PRYSPRY fold in chain B (shown in gray), whereas the equivalent structural elements of chain B are disordered. (B) Symmetrical dimer in the crystal structure of the TRIM36 PRYSPRY domain. The dimer interface is formed via the insertion connecting the canonical β-strands 2 and 3. (C) Size-exclusion chromatography of the TRIM11 and TRIM36 PRYSPRY domain on a Superdex-75 column compared with the elution profiles of marker proteins. TRIM11 eluted at a retention time corresponding to a monomer (orange trace; theoretical MW of the monomer = 20.9 kDa), whereas TRIM36 eluted at a retention time corresponding to a dimer, in agreement with the structural data (magenta trace; theoretical MW of the dimer = 52.4 kDa). Marker proteins used: bovine serum albumin (MW = 66 kDa; Sigma-Aldrich), hen egg white ovalbumin (MW = 44 kDa, Sigma-Aldrich), bovine <t>erythrocyte</t> carbonic <t>anhydrase</t> (MW = 30 kDa, MP Biomedicals), bovine ribonuclease A (MW = 13.7 kDa, Sigma-Aldrich).
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Structural differences in TRIM11 and TRIM36 PRYSPRY domains. (A) Asymmetric unit of the TRIM11 PRYSPRY structure showing subdomain swapping. β-strands 7 and 8 of chain A (shown in dark red) complete the canonical PRYSPRY fold in chain B (shown in gray), whereas the equivalent structural elements of chain B are disordered. (B) Symmetrical dimer in the crystal structure of the TRIM36 PRYSPRY domain. The dimer interface is formed via the insertion connecting the canonical β-strands 2 and 3. (C) Size-exclusion chromatography of the TRIM11 and TRIM36 PRYSPRY domain on a Superdex-75 column compared with the elution profiles of marker proteins. TRIM11 eluted at a retention time corresponding to a monomer (orange trace; theoretical MW of the monomer = 20.9 kDa), whereas TRIM36 eluted at a retention time corresponding to a dimer, in agreement with the structural data (magenta trace; theoretical MW of the dimer = 52.4 kDa). Marker proteins used: bovine serum albumin (MW = 66 kDa; Sigma-Aldrich), hen egg white ovalbumin (MW = 44 kDa, Sigma-Aldrich), bovine <t>erythrocyte</t> carbonic <t>anhydrase</t> (MW = 30 kDa, MP Biomedicals), bovine ribonuclease A (MW = 13.7 kDa, Sigma-Aldrich).
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human carbonic anhydrase ix  (Sino Biological)
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Structural differences in TRIM11 and TRIM36 PRYSPRY domains. (A) Asymmetric unit of the TRIM11 PRYSPRY structure showing subdomain swapping. β-strands 7 and 8 of chain A (shown in dark red) complete the canonical PRYSPRY fold in chain B (shown in gray), whereas the equivalent structural elements of chain B are disordered. (B) Symmetrical dimer in the crystal structure of the TRIM36 PRYSPRY domain. The dimer interface is formed via the insertion connecting the canonical β-strands 2 and 3. (C) Size-exclusion chromatography of the TRIM11 and TRIM36 PRYSPRY domain on a Superdex-75 column compared with the elution profiles of marker proteins. TRIM11 eluted at a retention time corresponding to a monomer (orange trace; theoretical MW of the monomer = 20.9 kDa), whereas TRIM36 eluted at a retention time corresponding to a dimer, in agreement with the structural data (magenta trace; theoretical MW of the dimer = 52.4 kDa). Marker proteins used: bovine serum albumin (MW = 66 kDa; Sigma-Aldrich), hen egg white ovalbumin (MW = 44 kDa, Sigma-Aldrich), bovine <t>erythrocyte</t> carbonic <t>anhydrase</t> (MW = 30 kDa, MP Biomedicals), bovine ribonuclease A (MW = 13.7 kDa, Sigma-Aldrich).
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Structural differences in TRIM11 and TRIM36 PRYSPRY domains. (A) Asymmetric unit of the TRIM11 PRYSPRY structure showing subdomain swapping. β-strands 7 and 8 of chain A (shown in dark red) complete the canonical PRYSPRY fold in chain B (shown in gray), whereas the equivalent structural elements of chain B are disordered. (B) Symmetrical dimer in the crystal structure of the TRIM36 PRYSPRY domain. The dimer interface is formed via the insertion connecting the canonical β-strands 2 and 3. (C) Size-exclusion chromatography of the TRIM11 and TRIM36 PRYSPRY domain on a Superdex-75 column compared with the elution profiles of marker proteins. TRIM11 eluted at a retention time corresponding to a monomer (orange trace; theoretical MW of the monomer = 20.9 kDa), whereas TRIM36 eluted at a retention time corresponding to a dimer, in agreement with the structural data (magenta trace; theoretical MW of the dimer = 52.4 kDa). Marker proteins used: bovine serum albumin (MW = 66 kDa; Sigma-Aldrich), hen egg white ovalbumin (MW = 44 kDa, Sigma-Aldrich), bovine erythrocyte carbonic anhydrase (MW = 30 kDa, MP Biomedicals), bovine ribonuclease A (MW = 13.7 kDa, Sigma-Aldrich).

Journal: Journal of Structural Biology: X

Article Title: Structural analysis of TRIM family PRYSPRY domains and its implications for E3-ligand design

doi: 10.1016/j.yjsbx.2025.100134

Figure Lengend Snippet: Structural differences in TRIM11 and TRIM36 PRYSPRY domains. (A) Asymmetric unit of the TRIM11 PRYSPRY structure showing subdomain swapping. β-strands 7 and 8 of chain A (shown in dark red) complete the canonical PRYSPRY fold in chain B (shown in gray), whereas the equivalent structural elements of chain B are disordered. (B) Symmetrical dimer in the crystal structure of the TRIM36 PRYSPRY domain. The dimer interface is formed via the insertion connecting the canonical β-strands 2 and 3. (C) Size-exclusion chromatography of the TRIM11 and TRIM36 PRYSPRY domain on a Superdex-75 column compared with the elution profiles of marker proteins. TRIM11 eluted at a retention time corresponding to a monomer (orange trace; theoretical MW of the monomer = 20.9 kDa), whereas TRIM36 eluted at a retention time corresponding to a dimer, in agreement with the structural data (magenta trace; theoretical MW of the dimer = 52.4 kDa). Marker proteins used: bovine serum albumin (MW = 66 kDa; Sigma-Aldrich), hen egg white ovalbumin (MW = 44 kDa, Sigma-Aldrich), bovine erythrocyte carbonic anhydrase (MW = 30 kDa, MP Biomedicals), bovine ribonuclease A (MW = 13.7 kDa, Sigma-Aldrich).

Article Snippet: Marker proteins used: bovine serum albumin (MW = 66 kDa; Sigma-Aldrich), hen egg white ovalbumin (MW = 44 kDa, Sigma-Aldrich), bovine erythrocyte carbonic anhydrase (MW = 30 kDa, MP Biomedicals), bovine ribonuclease A (MW = 13.7 kDa, Sigma-Aldrich).

Techniques: Size-exclusion Chromatography, Marker