![]() | This article may be too technical for most readers to understand.(July 2011) |
Adap_comp_sub | |||||||||
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![]() mu2 adaptin subunit (ap50) of ap2 adaptor (second domain), complexed with ctla-4 internalization peptide ttgvyvkmppt | |||||||||
Identifiers | |||||||||
Symbol | Adap_comp_sub | ||||||||
Pfam | PF00928 | ||||||||
Pfam clan | CL0448 | ||||||||
InterPro | IPR008968 | ||||||||
PROSITE | PDOC00761 | ||||||||
SCOP2 | 1bxx / SCOPe / SUPFAM | ||||||||
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In molecular biology, the adaptor complexes medium subunit domain is a protein domain found at the C-terminus of the mu subunit from various clathrin adaptor protein complexes (AP1, AP2, AP3, AP4 and AP5) [1] and muniscins. The C-terminal domain has an 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. [2] The mu subunit regulates the coupling of clathrin lattices with particular membrane proteins by self- phosphorylation via a mechanism that is still unclear. [3] The mu subunit possesses a 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. [3]
![]() | This article may be too technical for most readers to understand.(July 2011) |
Adap_comp_sub | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() mu2 adaptin subunit (ap50) of ap2 adaptor (second domain), complexed with ctla-4 internalization peptide ttgvyvkmppt | |||||||||
Identifiers | |||||||||
Symbol | Adap_comp_sub | ||||||||
Pfam | PF00928 | ||||||||
Pfam clan | CL0448 | ||||||||
InterPro | IPR008968 | ||||||||
PROSITE | PDOC00761 | ||||||||
SCOP2 | 1bxx / SCOPe / SUPFAM | ||||||||
|
In molecular biology, the adaptor complexes medium subunit domain is a protein domain found at the C-terminus of the mu subunit from various clathrin adaptor protein complexes (AP1, AP2, AP3, AP4 and AP5) [1] and muniscins. The C-terminal domain has an 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. [2] The mu subunit regulates the coupling of clathrin lattices with particular membrane proteins by self- phosphorylation via a mechanism that is still unclear. [3] The mu subunit possesses a 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. [3]