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molecular biology, the adaptor complexes medium subunit domain is a protein domain found at the C-terminus of the mu subunit from various clathrin adaptors (AP1, AP2 and AP3). The C-terminal domain has an [1 ] immunoglobulin-like beta-sandwich fold consisting of 9 strands in 2 sheets with a Greek key topology, similar to that found in cytochrome f and certain transcription factors. The mu subunit regulates the coupling of clathrin lattices with particular [1 ] membrane proteins by self- phosphorylation via a mechanism that is still unclear. The mu subunit possesses a [2 ] highly conserved N-terminal domain of around 230 amino acids, which may be the region of interaction with other AP proteins; a linker region of between 10 and 42 amino acids; and a less well-conserved C-terminal domain of around 190 amino acids, which may be the site of specific interaction with the protein being transported in the vesicle. [2 ]
^ a b Follows ER, McPheat JC, Minshull C, Moore NC, Pauptit RA, Rowsell S, Stacey CL, Stanway JJ, Taylor IW, Abbott WM (October 2001). "Study of the interaction of the medium chain mu 2 subunit of the clathrin-associated adapter protein complex 2 with cytotoxic T-lymphocyte antigen 4 and CD28". Biochem. J. 359 (Pt 2): 427–34. doi: 10.1042/0264-6021:3590427. PMC 1222163. PMID 11583591.
^ a b Nakayama Y, Goebl M, O'Brine Greco B, Lemmon S, Pingchang Chow E, Kirchhausen T (December 1991). "The medium chains of the mammalian clathrin-associated proteins have a homolog in yeast". Eur. J. Biochem. 202 (2): 569–74. doi: 10.1111/j.1432-1033.1991.tb16409.x. PMID 1761056.
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This article incorporates text from the public domain Pfam and InterPro IPR008968