Journal:MicroPubl Biol:000669
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When the <scene name='94/945523/Cv/7'>PH domain of human protein kinase B/Akt (in pink) containing a bound phosphatidylinositol trisphosphate ligand (shown in ball-in-sticks; PDB [[1h10]]) was overlaid with the GhVAB-A0A1U8N485 PH domain (in orange)</scene>, a deep binding pocket accommodating the phosphoinositide ligand was observed in the structure. Indeed, <scene name='94/945523/Cv/9'>this GhVAB-A0A1U8N485 binding pocket is lined with positively-charged amino acids that could interact with the negatively-charge phosphate groups</scene> ({{Template:ColorKey_Charge_Anionic}} / {{Template:ColorKey_Charge_Cationic}}) and <scene name='94/945523/Cv/14'>residues within this pocket are highly-conserved based on ConSurf analysis</scene>. | When the <scene name='94/945523/Cv/7'>PH domain of human protein kinase B/Akt (in pink) containing a bound phosphatidylinositol trisphosphate ligand (shown in ball-in-sticks; PDB [[1h10]]) was overlaid with the GhVAB-A0A1U8N485 PH domain (in orange)</scene>, a deep binding pocket accommodating the phosphoinositide ligand was observed in the structure. Indeed, <scene name='94/945523/Cv/9'>this GhVAB-A0A1U8N485 binding pocket is lined with positively-charged amino acids that could interact with the negatively-charge phosphate groups</scene> ({{Template:ColorKey_Charge_Anionic}} / {{Template:ColorKey_Charge_Cationic}}) and <scene name='94/945523/Cv/14'>residues within this pocket are highly-conserved based on ConSurf analysis</scene>. | ||
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A structure-based alignment between GhVAB-A0A1U8N485 and human protein kinase B/Akt indicated that two of the five ligand-binding residues in B/Akt are completely conserved in GhVAB-A0A1U8N485, with two others being conservative substitutions (Thomas ''et al''., 2002<ref name='Thomas'>PMID: 12176338</ref>). Evidence from sequence and structure features support that GhVAB-A0A1U8N485 is part of the VAN3-binding protein family. Furthermore, based on functional reports of other VAN3-binding proteins as well as structural analysis of our protein, GhVAB-A0A1U8N485 might be involved in regulating leaf size or vein development in cotton plants by binding phosphoinositides as part of an auxin signaling pathway. | A structure-based alignment between GhVAB-A0A1U8N485 and human protein kinase B/Akt indicated that two of the five ligand-binding residues in B/Akt are completely conserved in GhVAB-A0A1U8N485, with two others being conservative substitutions (Thomas ''et al''., 2002<ref name='Thomas'>PMID: 12176338</ref>). Evidence from sequence and structure features support that GhVAB-A0A1U8N485 is part of the VAN3-binding protein family. Furthermore, based on functional reports of other VAN3-binding proteins as well as structural analysis of our protein, GhVAB-A0A1U8N485 might be involved in regulating leaf size or vein development in cotton plants by binding phosphoinositides as part of an auxin signaling pathway. | ||
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