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[[Image:1iu1.jpg|left|200px]]
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{{STRUCTURE_1iu1|  PDB=1iu1  |  SCENE=  }}
'''Crystal structure of human gamma1-adaptin ear domain'''


==Crystal structure of human gamma1-adaptin ear domain==
<StructureSection load='1iu1' size='340' side='right'caption='[[1iu1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iu1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IU1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1iu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iu1 OCA], [https://pdbe.org/1iu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iu1 RCSB], [https://www.ebi.ac.uk/pdbsum/1iu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iu1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AP1G1_HUMAN AP1G1_HUMAN] 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iu/1iu1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1iu1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The adaptor proteins AP-1 and GGA regulate membrane traffic between the trans-Golgi network (TGN) and endosomes/lysosomes through ARF-regulated membrane association, recognition of sorting signals, and recruitment of clathrin and accessory proteins. The gamma 1-adaptin subunits of AP-1 and GGA possess homologous ear domains involved in the recruitment of accessory proteins, gamma-synergin and Rabaptin-5. The crystal structure of the human gamma 1-adaptin ear domain consists solely of an immunoglobulin-like fold, unlike the alpha-adaptin ear domain. Structure-based mutational analyses reveal a binding site for the accessory proteins that is composed of conserved basic residues, indicating that the recruitment mechanism in gamma 1-adaptin and GGA is distinct from that in alpha-adaptin.


==Overview==
Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain.,Nogi T, Shiba Y, Kawasaki M, Shiba T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Takatsu H, Nakayama K, Wakatsuki S Nat Struct Biol. 2002 Jul;9(7):527-31. PMID:12042876<ref>PMID:12042876</ref>
The adaptor proteins AP-1 and GGA regulate membrane traffic between the trans-Golgi network (TGN) and endosomes/lysosomes through ARF-regulated membrane association, recognition of sorting signals, and recruitment of clathrin and accessory proteins. The gamma 1-adaptin subunits of AP-1 and GGA possess homologous ear domains involved in the recruitment of accessory proteins, gamma-synergin and Rabaptin-5. The crystal structure of the human gamma 1-adaptin ear domain consists solely of an immunoglobulin-like fold, unlike the alpha-adaptin ear domain. Structure-based mutational analyses reveal a binding site for the accessory proteins that is composed of conserved basic residues, indicating that the recruitment mechanism in gamma 1-adaptin and GGA is distinct from that in alpha-adaptin.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1IU1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU1 OCA].
</div>
<div class="pdbe-citations 1iu1" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain., Nogi T, Shiba Y, Kawasaki M, Shiba T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Takatsu H, Nakayama K, Wakatsuki S, Nat Struct Biol. 2002 Jul;9(7):527-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12042876 12042876]
*[[Adaptin 3D structures|Adaptin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Igarashi, N.]]
[[Category: Igarashi N]]
[[Category: Kato, R.]]
[[Category: Kato R]]
[[Category: Kawasaki, M.]]
[[Category: Kawasaki M]]
[[Category: Matsugaki, N.]]
[[Category: Matsugaki N]]
[[Category: Nakayama, K.]]
[[Category: Nakayama K]]
[[Category: Nogi, T.]]
[[Category: Nogi T]]
[[Category: Shiba, T.]]
[[Category: Shiba T]]
[[Category: Shiba, Y.]]
[[Category: Shiba Y]]
[[Category: Suzuki, M.]]
[[Category: Suzuki M]]
[[Category: Takatsu, H.]]
[[Category: Takatsu H]]
[[Category: Wakatsuki, S.]]
[[Category: Wakatsuki S]]
[[Category: Coated pit]]
[[Category: Endocytosis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:35:49 2008''