2vgl
From Proteopedia
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[[Image:2vgl.jpg|left|200px]] | [[Image:2vgl.jpg|left|200px]] | ||
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- | + | {{STRUCTURE_2vgl| PDB=2vgl | SCENE= }} | |
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'''AP2 CLATHRIN ADAPTOR CORE''' | '''AP2 CLATHRIN ADAPTOR CORE''' | ||
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==About this Structure== | ==About this Structure== | ||
- | 2VGL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry | + | 2VGL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gw5 1gw5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mccoy, A J.]] | [[Category: Mccoy, A J.]] | ||
[[Category: Owen, D J.]] | [[Category: Owen, D J.]] | ||
- | [[Category: | + | [[Category: Adaptor]] |
- | [[Category: | + | [[Category: Alternative splicing]] |
- | [[Category: | + | [[Category: Coated pit]] |
- | [[Category: | + | [[Category: Cytoplasmic vesicle]] |
- | [[Category: | + | [[Category: Endocytosis]] |
- | [[Category: | + | [[Category: Golgi apparatus]] |
- | [[Category: | + | [[Category: Lipid-binding]] |
- | [[Category: | + | [[Category: Membrane]] |
- | [[Category: | + | [[Category: Phosphorylation]] |
- | [[Category: | + | [[Category: Protein transport]] |
- | [[Category: | + | [[Category: Transport]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:46:08 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:46, 4 May 2008
AP2 CLATHRIN ADAPTOR CORE
Overview
AP2 is the best-characterized member of the family of heterotetrameric clathrin adaptor complexes that play pivotal roles in many vesicle trafficking pathways within the cell. AP2 functions in clathrin-mediated endocytosis, the process whereby cargo enters the endosomal system from the plasma membrane. We describe the structure of the 200 kDa AP2 "core" (alpha trunk, beta2 trunk, mu2, and sigma2) complexed with the polyphosphatidylinositol headgroup mimic inositolhexakisphosphate at 2.6 A resolution. Two potential polyphosphatidylinositide binding sites are observed, one on alpha and one on mu2. The binding site for Yxxphi endocytic motifs is buried, indicating that a conformational change, probably triggered by phosphorylation in the disordered mu2 linker, is necessary to allow Yxxphi motif binding. A model for AP2 recruitment and activation is proposed.
About this Structure
2VGL is a Protein complex structure of sequences from Homo sapiens, Mus musculus and Rattus norvegicus. This structure supersedes the now removed PDB entry 1gw5. Full crystallographic information is available from OCA.
Reference
Molecular architecture and functional model of the endocytic AP2 complex., Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ, Cell. 2002 May 17;109(4):523-35. PMID:12086608 Page seeded by OCA on Sun May 4 18:46:08 2008
Categories: Homo sapiens | Mus musculus | Protein complex | Rattus norvegicus | Collins, B M. | Evans, P R. | Mccoy, A J. | Owen, D J. | Adaptor | Alternative splicing | Coated pit | Cytoplasmic vesicle | Endocytosis | Golgi apparatus | Lipid-binding | Membrane | Phosphorylation | Protein transport | Transport