4nee

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==crystal structure of AP-2 alpha/simga2 complex bound to HIV-1 Nef==
==crystal structure of AP-2 alpha/simga2 complex bound to HIV-1 Nef==
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<StructureSection load='4nee' size='340' side='right' caption='[[4nee]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
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<StructureSection load='4nee' size='340' side='right'caption='[[4nee]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nee]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1] and [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NEE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nee]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NEE FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nee OCA], [https://pdbe.org/4nee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nee RCSB], [https://www.ebi.ac.uk/pdbsum/4nee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nee ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ap2s1, Ap17, Claps2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Ap17, Ap2a2, Ap2s1, Claps2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), nef ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nee OCA], [http://pdbe.org/4nee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nee RCSB], [http://www.ebi.ac.uk/pdbsum/4nee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nee ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AP2S1_RAT AP2S1_RAT]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein Transport via Transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. May also play a role in extracellular calcium homeostasis (By similarity).<ref>PMID:14745134</ref> <ref>PMID:15473838</ref>
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[https://www.uniprot.org/uniprot/AP2S1_RAT AP2S1_RAT] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein Transport via Transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. May also play a role in extracellular calcium homeostasis (By similarity).<ref>PMID:14745134</ref> <ref>PMID:15473838</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Adaptin|Adaptin]]
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*[[Adaptin 3D structures|Adaptin 3D structures]]
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*[[Protein Nef|Protein Nef]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
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[[Category: Human immunodeficiency virus 1]]
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[[Category: Bonifacino, J S]]
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[[Category: Large Structures]]
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[[Category: Hurley, J H]]
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[[Category: Rattus norvegicus]]
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[[Category: Park, S Y]]
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[[Category: Bonifacino JS]]
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[[Category: Ren, X]]
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[[Category: Hurley JH]]
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[[Category: Cd4 downregulation]]
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[[Category: Park SY]]
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[[Category: Clathrin adaptor ap-2]]
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[[Category: Ren X]]
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[[Category: Hiv-1 nef]]
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[[Category: Viral protein-protein transport complex]]
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Revision as of 08:25, 11 January 2023

crystal structure of AP-2 alpha/simga2 complex bound to HIV-1 Nef

PDB ID 4nee

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