unresolved region Search Results


unresolved region  (Addgene inc)
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(A) Three-dimensional structure of bovine RPE65 (PDB ID: 3FSN ). The crystallographically <t>unresolved</t> (aa107–125) region of RPE65 protein, modeled using I-TASSER server, is shown in red color. (B) Alignment of RPE65 aa107–125 from several jawed and jawless vertebrate taxa showing sequence conservation throughout evolution. (C) Helical wheel representation of the crystallographically unresolved aa107–125 region of RPE65 protein using HELIQUEST server. (D) Predicted secondary structure, relative accessibility and hydropathy analysis of the aa107–125 region of RPE65 protein using I-TASSER and ENDScript server, respectively. (E) Hydropathic moment plot of combined 35 different RPE65 aa107–125 and paralogous conserved region sequences from vertebrate and non-vertebrate carotenoid cleavage dioxygenase (CCD) paralogs, derived from HeliQuest . Red stars, RPE65 s; magenta circles, vertebrate BCO1s; blue circles, vertebrate BCO2s; black circle, early chordate ( Ciona ) CCD; yellow circles, arthropod ( Trinorchestia , Palaemon , Drosophila , and Galleria ) CCDs; and green circles, nematode ( Caenorhabditis ) -CCDs. Note tight grouping of all 10 RPE65 s distinct from other paralogs. (F) Physicochemical properties of the crystallographically unresolved (aa107–125) of RPE65 protein. Abbreviations: acc, accessibility; hyd, hydrophobicity.
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(A) Three-dimensional structure of bovine RPE65 (PDB ID: 3FSN ). The crystallographically unresolved (aa107–125) region of RPE65 protein, modeled using I-TASSER server, is shown in red color. (B) Alignment of RPE65 aa107–125 from several jawed and jawless vertebrate taxa showing sequence conservation throughout evolution. (C) Helical wheel representation of the crystallographically unresolved aa107–125 region of RPE65 protein using HELIQUEST server. (D) Predicted secondary structure, relative accessibility and hydropathy analysis of the aa107–125 region of RPE65 protein using I-TASSER and ENDScript server, respectively. (E) Hydropathic moment plot of combined 35 different RPE65 aa107–125 and paralogous conserved region sequences from vertebrate and non-vertebrate carotenoid cleavage dioxygenase (CCD) paralogs, derived from HeliQuest . Red stars, RPE65 s; magenta circles, vertebrate BCO1s; blue circles, vertebrate BCO2s; black circle, early chordate ( Ciona ) CCD; yellow circles, arthropod ( Trinorchestia , Palaemon , Drosophila , and Galleria ) CCDs; and green circles, nematode ( Caenorhabditis ) -CCDs. Note tight grouping of all 10 RPE65 s distinct from other paralogs. (F) Physicochemical properties of the crystallographically unresolved (aa107–125) of RPE65 protein. Abbreviations: acc, accessibility; hyd, hydrophobicity.

Journal: Life Science Alliance

Article Title: An inducible amphipathic α-helix mediates subcellular targeting and membrane binding of RPE65

doi: 10.26508/lsa.202201546

Figure Lengend Snippet: (A) Three-dimensional structure of bovine RPE65 (PDB ID: 3FSN ). The crystallographically unresolved (aa107–125) region of RPE65 protein, modeled using I-TASSER server, is shown in red color. (B) Alignment of RPE65 aa107–125 from several jawed and jawless vertebrate taxa showing sequence conservation throughout evolution. (C) Helical wheel representation of the crystallographically unresolved aa107–125 region of RPE65 protein using HELIQUEST server. (D) Predicted secondary structure, relative accessibility and hydropathy analysis of the aa107–125 region of RPE65 protein using I-TASSER and ENDScript server, respectively. (E) Hydropathic moment plot of combined 35 different RPE65 aa107–125 and paralogous conserved region sequences from vertebrate and non-vertebrate carotenoid cleavage dioxygenase (CCD) paralogs, derived from HeliQuest . Red stars, RPE65 s; magenta circles, vertebrate BCO1s; blue circles, vertebrate BCO2s; black circle, early chordate ( Ciona ) CCD; yellow circles, arthropod ( Trinorchestia , Palaemon , Drosophila , and Galleria ) CCDs; and green circles, nematode ( Caenorhabditis ) -CCDs. Note tight grouping of all 10 RPE65 s distinct from other paralogs. (F) Physicochemical properties of the crystallographically unresolved (aa107–125) of RPE65 protein. Abbreviations: acc, accessibility; hyd, hydrophobicity.

Article Snippet: We cloned the crystallographically unresolved region (107–125 aa, AH 107-125 ) of RPE65 protein into the MBP fusion cloning vector pET His6 MBP TEV LIC (2M-T; a gift from Scott Gradia, plasmid # 29708; Addgene).

Techniques: Sequencing, Derivative Assay