|
Lysosome-associated membrane glycoproteins (lamp) are integral membrane proteins, specific to lysosomes, and whose exact biological function is not yet clear. Structurally, the lamp proteins consist of two internally homologous lysosome-luminal domains separated by a proline-rich hinge region; at the C-terminal extremity there is a transmembrane region (TM) followed by a very short cytoplasmic tail (C). In each of the duplicated domains, there are two conserved disulfide bonds. This structure is schematically represented in the figure below. +-----+ +-----+ +-----+ +-----+ | | | | | | | | +--------------------------++Hinge++--------------------------++TM++C+ In mammals, there are two closely related types of lamp: LAMP1 and LAMP2. CD69 (also called gp110 or macrosialin) is a heavily glycosylated integral membrane protein whose structure consists of a mucin-like domain followed by a proline-rich hinge; a single lamp-like domain; a transmembrane region and a short cytoplasmic tail. CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at Protein Reviews On The Web (http://mpr.nci.nih.gov/prow/). ==Human proteins containing this domain == CD68; LAMP1; LAMP2; LAMP3; 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「Lysosome-associated membrane glycoprotein」の詳細全文を読む スポンサード リンク
|