Adaptin: Difference between revisions

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</StructureSection>
</StructureSection>


===3D structures of adaptin===


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*AP-α-2
**[[1b9k]], [[1qts]] – mAP appendage domain – mouse<br />
**[[1qtp]] – mAP appendage domain (mutant)<br />
**[[1ky6]], [[1kyd]] – mAP appendage domain + epsin peptide<br />
**[[1ky7]] – mAP appendage domain + amphiphysin peptide<br />
**[[1kyf]], [[1kyu]] – mAP appendage domain + eps15 peptide<br />
**[[1w80]], [[2vj0]] – mAP appendage domain + synaptojanin peptide<br />
**[[3hs8]] – mAP appendage domain + intersectin peptide<br />
*AP-β
**[[1e42]] – hAP-1 appendage domain - human<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 />
**[[1mj7]] – hAP-4 appendage domain <br />
*AP-γ
**[[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-1
**[[4afi]] – hAP-1/vesicle-associated membrane protein 7<br />
*AP-μ
**[[3h85]] – rAP-1 appendage domain + PTDINSPKIγ peptide<br />
**[[4emz]], [[4en2]] – mAP-1 sorting motif recognition domain + nef + MHC-I<br />
**[[2bp5]] – rAP-2 + purinoceptor peptide<br />
**[[1bw8]], [[1i31]] – rAP-2 C-terminal + EGFR peptide<br />
**[[1bxx]] – rAP-2 C-terminal + TGN38 peptide<br />
**[[1hes]] – rAP-2 C-terminal + selectin peptide<br />
**[[5c7z]], [[5fpi]] – rAP-2 C terminal + integrin peptide<br />
**[[2pr9]] – rAP-2 C-terminal + GABA receptor peptide<br />
**[[5wrm]], [[5wrl]], [[5wrk]] – rAP-2 C-terminal + insulin receptor substrate peptide <br />
**[[4ikn]] – rAP-3 + TGN38 sorting peptide <br />
**[[3l81]], [[4mdr]] – hAP-4 + amyloid beta-A4 peptide <br />
**[[6bnt]] – hAP-2 C-terminal + insulin receptor substrate peptide <br />
*AP-α2 + AP-σ
**[[4nee]] – rAP-2 + HIV-1 NEF <br />
*AP-α2 + AP-β + AP-σ
**[[4uqi]] – rAP-2 + VPU <br />
*AP-α + AP-β + AP-μ + AP-σ
**[[2vgl]] – rAPα-2 + APβ-1 + APμ-1 + APσ-1 <br />
**[[4uqi]] – rAPα-2 + APβ-2 + APμ-2 + APσ-1 <br />
**[[2jkr]], [[2jkt]] – mAPα-2 + APβ-1 + APμ-1 + APσ-1 + CD4 peptide<br />
**[[2xa7]] – rAPα-2 + APβ + APμ + APσ + cargo peptide<br />
*AP-β-1 + AP-γ-1 + AP-μ-1 + AP-σ-3
**[[6dff]], [[6d84]], [[6d83]], [[6cri]], [[6cm9]] – hAPβ-1 + APμ-1 + APσ-3 + ARF1 + tetherin-NEF – Cryo EM <br />
*AP-γ + AP-β + AP-μ + AP-σ
**[[1w63]] – mAP-1  <br />
**[[4hmy]] – mAP-1 + ADP-ribosylation factor<br />
**[[4p6z]] – mAP-1 + VPU + bone marrow stromal antigen<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 11:58, 28 February 2019

Adaptin (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits. The AP complex is a heterotetramer 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.[1]

3D structures of adaptin

Adaptin 3D structures


Structure of Adaptin core: AP-α-2 (cyan), AP-β-1 (magenta), AP-μ-1 (green), AP-σ-1 (olive) complex with inositole hexakisphosphate (PDB entry 2vgl)

Drag the structure with the mouse to rotate


ReferencesReferences

  1. ↑ 1.0 1.1 Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. Molecular architecture and functional model of the endocytic AP2 complex. Cell. 2002 May 17;109(4):523-35. PMID:12086608

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Michal Harel, Alexander Berchansky
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