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HHV Capsid Portal Protein, or HSV-1 UL-6 protein, is the protein which forms a cylindrical portal in the capsid of Herpes simplex virus (HSV-1). The protein is commonly referred to as the ''HSV-1 UL-6'' protein because it is the transcription product of Herpes gene UL-6. The Herpes viral DNA enters and exits the capsid via the capsid portal. The capsid portal is formed by twelve copies of portal protein arranged as a ring; the proteins contain a leucine zipper sequence of amino acids which allow them to adhere to each other.〔 〕 Each icosahedral capsid contains a single portal, located in one vertex.〔(Article: ()) 〕〔 〕 The portal is formed during initial capsid assembly and interacts with ''scaffolding proteins'' that construct the procapsid.〔 〕 〔 (Article: ()) 〕 〔 〕 When the capsid is nearly complete, the viral DNA enters the capsid (i.e., the DNA is ''encapsidated'') by a mechanism involving the portal and a DNA-binding protein complex similar to bacteriophage terminase.〔 〕 Multiple studies suggest an evolutionary relationship between Capsid Portal Protein and bacteriophage portal proteins.〔〔 When virus infects a cell, it is necessary for the viral DNA to be released from the capsid. The Herpes virus DNA exits through the capsid portal.〔 〕 The genetic sequence of HSV-1 gene UL-6 is conserved across the Herpesviridae family and this family of genes is known as the "Herpesvirus UL6-like" gene family.〔(Herpesvirus UL6 like Conserved Domains view at NCBI )〕 "UL-6" is nomenclature meaning that the protein is genetically encoded by the sixth (6th) open reading frame found in the viral genome segment named "Unique-Long (UL)". ==Studies== 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「HHV capsid portal protein」の詳細全文を読む スポンサード リンク
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