1gyv

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[[Image:1gyv.jpg|left|200px]]
 
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{{Structure
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==Gamma-adaptin appendage domain from clathrin adaptor AP1, L762E mutant==
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|PDB= 1gyv |SIZE=350|CAPTION= <scene name='initialview01'>1gyv</scene>, resolution 1.71&Aring;
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<StructureSection load='1gyv' size='340' side='right'caption='[[1gyv]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1gyv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYV FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.71&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyv OCA], [https://pdbe.org/1gyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gyv RCSB], [https://www.ebi.ac.uk/pdbsum/1gyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyv ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AP1G1_MOUSE AP1G1_MOUSE] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gyv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gyv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The AP1 complex is one of a family of heterotetrameric clathrin-adaptor complexes involved in vesicular trafficking between the Golgi and endosomes. The complex has two large subunits, gamma and beta1, which can be divided into trunk, hinge, and appendage domains. The 1.8 A resolution structure of the gamma appendage is presented. The binding site for the known gamma appendage ligand gamma-synergin is mapped through creation of point mutations designed on the basis of the structure. We also show that Eps15, a protein believed to be involved in vesicle formation at the plasma membrane, is also a ligand of gamma appendage and binds to the same site as gamma-synergin. This observation explains the demonstrated brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi complex.
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'''GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1, L762E MUTANT'''
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Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin.,Kent HM, McMahon HT, Evans PR, Benmerah A, Owen DJ Structure. 2002 Aug;10(8):1139-48. PMID:12176391<ref>PMID:12176391</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1gyv" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The AP1 complex is one of a family of heterotetrameric clathrin-adaptor complexes involved in vesicular trafficking between the Golgi and endosomes. The complex has two large subunits, gamma and beta1, which can be divided into trunk, hinge, and appendage domains. The 1.8 A resolution structure of the gamma appendage is presented. The binding site for the known gamma appendage ligand gamma-synergin is mapped through creation of point mutations designed on the basis of the structure. We also show that Eps15, a protein believed to be involved in vesicle formation at the plasma membrane, is also a ligand of gamma appendage and binds to the same site as gamma-synergin. This observation explains the demonstrated brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi complex.
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*[[Adaptin 3D structures|Adaptin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1GYV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYV OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin., Kent HM, McMahon HT, Evans PR, Benmerah A, Owen DJ, Structure. 2002 Aug;10(8):1139-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12176391 12176391]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Evans PR]]
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[[Category: Evans, P R.]]
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[[Category: Kent HM]]
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[[Category: Kent, H M.]]
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[[Category: McMahon HM]]
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[[Category: Mcmahon, H M.]]
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[[Category: Owen DJ]]
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[[Category: Owen, D J.]]
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[[Category: adaptin]]
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[[Category: adaptor]]
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[[Category: clathrin]]
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[[Category: endocytosis]]
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[[Category: golgi]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:29:52 2008''
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Current revision

Gamma-adaptin appendage domain from clathrin adaptor AP1, L762E mutant

PDB ID 1gyv

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