Adaptin: Difference between revisions
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<StructureSection load='2vgl' size='350' side='right' caption='Structure of Adaptin core: AP-α (grey), AP-β (light green), AP-μ (green), AP-σ (olive green) complex with inositole hexakisphosphate (PDB entry [[2vgl]])' scene=''> | <StructureSection load='2vgl' size='350' side='right' caption='Structure of Adaptin core: AP-α-2 (grey), AP-β-1 (light green), AP-μ-1 (green), AP-σ-1 (olive green) complex with inositole hexakisphosphate (PDB entry [[2vgl]])' scene=''> | ||
'''Adaptin''' (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits. The AP complex is a hetertetramer composed of 2 large AP: AP-α or AP-γ and AP-β, a medium-size AP: AP-μ and small AP: AP-σ. AP complexes connect proteins and lipids to clathrin budding sites. There are different AP complexes in mammals. | '''Adaptin''' (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits. The AP complex is a hetertetramer composed of 2 large AP: AP-α or AP-γ and AP-β, a medium-size AP: AP-μ and small AP: AP-σ. AP complexes connect proteins and lipids to clathrin budding sites. There are different AP complexes in mammals. | ||
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
'''AP-α''' | '''AP-α-2''' | ||
[[1b9x]], [[1qts]] – mAP appendage domain – mouse<br /> | [[1b9x]], [[1qts]] – mAP appendage domain – mouse<br /> | ||
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'''AP-β''' | '''AP-β''' | ||
[[1e42]] - | [[1e42]] – hAP-1 appendage domain - human<br /> | ||
[[2g30]] – hAP appendage domain + ARH peptide<br /> | [[2g30]] – hAP-1 appendage domain + ARH peptide<br /> | ||
[[ | [[3h1z]] – hAP-1 appendage domain + PTDINSPKI-γ peptide<br /> | ||
[[ | [[3hs9]] – hAP-1 appendage domain + intersectin peptide<br /> | ||
[[ | [[2iv9]] – hAP-2 appendage domain + eps15 peptide<br /> | ||
[[ | [[2iv8]] – hAP-2 appendage domain + B-arrestin peptide<br /> | ||
'''AP-γ''' | '''AP-γ''' | ||
[[1iu1]] | [[1iu1]] – hAP-1 ear domain<br /> | ||
[[ | [[1gyu]], [[2a7b]] – mAP-1 appendage domain <br /> | ||
[[ | [[1gyv]], [[1gyw]], [[3zy7]] – mAP-1 appendage domain (mutant)<br /> | ||
[[ | [[2e9g]], [[4bcx]] – hAP-2 ear domain<br /> | ||
[[ | [[2ymt]] – hAP-2 ear domain + peptide<br /> | ||
[[3zhf]] – hAP-2 ear domain + large envelope protein peptide<br /> | |||
'''AP-δ''' | '''AP-δ-1''' | ||
[[4afi]] – hAP/vesicle-associated membrane protein 7<br /> | [[4afi]] – hAP-1/vesicle-associated membrane protein 7<br /> | ||
'''AP-μ''' | '''AP-μ''' | ||
[[ | [[3h85]] – rAP-1 appendage domain + PTDINSPKIγ peptide<br /> | ||
[[ | [[4emz]], [[4en2]] – mAP-1 sorting motif recognition domain + nef + MHC-I<br /> | ||
[[ | [[1bw8]], [[1i31]] – rAP-2 + EGFR peptide<br /> | ||
[[ | [[1bxx]] – rAP-2 + TGN38 peptide<br /> | ||
[[ | [[1hes]] – rAP-2 + selectin peptide<br /> | ||
[[ | [[2bp5]] – rAP-2 + purinoceptor peptide<br /> | ||
[[ | [[2pr9]] – rAP-2 + GABA receptor peptide<br /> | ||
'''AP-α + AP-β + AP-μ + AP-σ''' | '''AP-α + AP-β + AP-μ + AP-σ''' | ||
[[2vgl]] – rAPα + APβ + APμ + APσ <br /> | [[2vgl]] – rAPα-2 + APβ-1 + APμ-1 + APσ-1 <br /> | ||
[[2jkr]], [[2jkt]] – mAPα + APβ + APμ + APσ + CD4 peptide<br /> | [[2jkr]], [[2jkt]] – mAPα-2 + APβ-1 + APμ-1 + APσ-1 + CD4 peptide<br /> | ||
[[2xa7]] – rAPα + APβ + APμ + APσ + cargo peptide<br /> | [[2xa7]] – rAPα-2 + APβ + APμ + APσ + cargo peptide<br /> | ||
'''AP-γ + AP-β + AP-μ + AP-σ''' | '''AP-γ + AP-β + AP-μ + AP-σ''' | ||
[[1w63]] – mAPγ + APβ + APμ + APσ <br /> | [[1w63]] – mAPγ-1 + APβ-1 + APμ-1 + APσ-1A <br /> | ||
[[4hmy]] – mAPγ + APβ + APμ + APσ + ADP-ribosylation factor<br /> | [[4hmy]] – mAPγ-1 + APβ-1 + APμ-1 + APσ-3 + ADP-ribosylation factor<br /> | ||
[[Category:Topic Page]] | |||
Revision as of 06:40, 30 June 2014
<StructureSection load='2vgl' size='350' side='right' caption='Structure of Adaptin core: AP-α-2 (grey), AP-β-1 (light green), AP-μ-1 (green), AP-σ-1 (olive green) complex with inositole hexakisphosphate (PDB entry 2vgl)' scene=> Adaptin (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits. The AP complex is a hetertetramer composed of 2 large AP: AP-α or AP-γ and AP-β, a medium-size AP: AP-μ and small AP: AP-σ. AP complexes connect proteins and lipids to clathrin budding sites. There are different AP complexes in mammals.
3D structures of adaptin
Updated on 30-June-2014
AP-α-2
1b9x, 1qts – mAP appendage domain – mouse
1qtp – mAP appendage domain (mutant)
1ky6, 1kyd – mAP appendage domain + epsin peptide
1ky7 – mAP appendage domain + amphiphysin peptide
1kyf, 1kyu – mAP appendage domain + eps15 peptide
1w80, 2vj0 – mAP appendage domain + synaptojanin peptide
3hs8 – mAP appendage domain + intersectin peptide
AP-β
1e42 – hAP-1 appendage domain - human
2g30 – hAP-1 appendage domain + ARH peptide
3h1z – hAP-1 appendage domain + PTDINSPKI-γ peptide
3hs9 – hAP-1 appendage domain + intersectin peptide
2iv9 – hAP-2 appendage domain + eps15 peptide
2iv8 – hAP-2 appendage domain + B-arrestin peptide
AP-γ
1iu1 – hAP-1 ear domain
1gyu, 2a7b – mAP-1 appendage domain
1gyv, 1gyw, 3zy7 – mAP-1 appendage domain (mutant)
2e9g, 4bcx – hAP-2 ear domain
2ymt – hAP-2 ear domain + peptide
3zhf – hAP-2 ear domain + large envelope protein peptide
AP-δ-1
4afi – hAP-1/vesicle-associated membrane protein 7
AP-μ
3h85 – rAP-1 appendage domain + PTDINSPKIγ peptide
4emz, 4en2 – mAP-1 sorting motif recognition domain + nef + MHC-I
1bw8, 1i31 – rAP-2 + EGFR peptide
1bxx – rAP-2 + TGN38 peptide
1hes – rAP-2 + selectin peptide
2bp5 – rAP-2 + purinoceptor peptide
2pr9 – rAP-2 + GABA receptor peptide
AP-α + AP-β + AP-μ + AP-σ
2vgl – rAPα-2 + APβ-1 + APμ-1 + APσ-1
2jkr, 2jkt – mAPα-2 + APβ-1 + APμ-1 + APσ-1 + CD4 peptide
2xa7 – rAPα-2 + APβ + APμ + APσ + cargo peptide
AP-γ + AP-β + AP-μ + AP-σ
1w63 – mAPγ-1 + APβ-1 + APμ-1 + APσ-1A
4hmy – mAPγ-1 + APβ-1 + APμ-1 + APσ-3 + ADP-ribosylation factor
