1jwf
From Proteopedia
(Difference between revisions)
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<StructureSection load='1jwf' size='340' side='right'caption='[[1jwf]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1jwf' size='340' side='right'caption='[[1jwf]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1jwf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1jwf]] is a 1 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=1JWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWF FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=1jwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwf OCA], [https://pdbe.org/1jwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwf RCSB], [https://www.ebi.ac.uk/pdbsum/1jwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwf ProSAT]</span></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=1jwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwf OCA], [https://pdbe.org/1jwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwf RCSB], [https://www.ebi.ac.uk/pdbsum/1jwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/GGA1_HUMAN GGA1_HUMAN] Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.<ref>PMID:11301005</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1jwf ConSurf]. | </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=1jwf ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | GGAs (Golgi-localizing, gamma-adaptin ear homology domain, ARF-interacting proteins) are critical for the transport of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF), and clathrin. The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster dileucine (ACLL) sequences. Here we report the X-ray structure of the GGA1 VHS domain alone, and in complex with the carboxy-terminal peptide of cation-independent mannose 6-phosphate receptor containing an ACLL sequence. The VHS domain forms a super helix with eight alpha-helices, similar to the VHS domains of TOM1 and Hrs. Unidirectional movements of helices alpha6 and alpha8, and some of their side chains, create a set of electrostatic and hydrophobic interactions for correct recognition of the ACLL peptide. This recognition mechanism provides the basis for regulation of protein transport from the TGN to endosomes/lysosomes, which is shared by sortilin and low-density lipoprotein receptor-related protein. | ||
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- | Structural basis for recognition of acidic-cluster dileucine sequence by GGA1.,Shiba T, Takatsu H, Nogi T, Matsugaki N, Kawasaki M, Igarashi N, Suzuki M, Kato R, Earnest T, Nakayama K, Wakatsuki S Nature. 2002 Feb 21;415(6874):937-41. PMID:11859376<ref>PMID:11859376</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1jwf" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Earnest | + | [[Category: Earnest T]] |
- | [[Category: Igarashi | + | [[Category: Igarashi N]] |
- | [[Category: Kato | + | [[Category: Kato R]] |
- | [[Category: Kawasaki | + | [[Category: Kawasaki M]] |
- | [[Category: Matsugaki | + | [[Category: Matsugaki N]] |
- | [[Category: Nakayama | + | [[Category: Nakayama K]] |
- | [[Category: Nogi | + | [[Category: Nogi T]] |
- | [[Category: Shiba | + | [[Category: Shiba T]] |
- | [[Category: Suzuki | + | [[Category: Suzuki M]] |
- | [[Category: Takatsu | + | [[Category: Takatsu H]] |
- | [[Category: Wakatsuki | + | [[Category: Wakatsuki S]] |
- | + | ||
- | + |
Revision as of 07:55, 3 April 2024
Crystal Structure of human GGA1 VHS domain.
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Categories: Homo sapiens | Large Structures | Earnest T | Igarashi N | Kato R | Kawasaki M | Matsugaki N | Nakayama K | Nogi T | Shiba T | Suzuki M | Takatsu H | Wakatsuki S