1p4u

<table><tr><td colspan='2'>[[1p4u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P4U FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GGA3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4u OCA], [http://pdbe.org/1p4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p4u RCSB], [http://www.ebi.ac.uk/pdbsum/1p4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p4u ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/GGA3_HUMAN GGA3_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> [[http://www.uniprot.org/uniprot/RABE1_HUMAN RABE1_HUMAN]] Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A.<ref>PMID:8521472</ref> <ref>PMID:10698684</ref> <ref>PMID:11452015</ref> <ref>PMID:12773381</ref>

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== Publication Abstract from PubMed ==

Adaptor proteins load transmembrane protein cargo into transport vesicles and serve as nexuses for the formation of large multiprotein complexes on the nascent vesicles. The gamma-adaptin ear (GAE) domains of the AP-1 adaptor protein complex and the GGA adaptor proteins recruit accessory proteins to these multiprotein complexes by binding to a hydrophobic motif. We determined the structure of the GAE domain of human GGA3 in complex with a peptide based on the DFGPLV sequence of the accessory protein Rabaptin-5 and refined it at a resolution of 2.2 A. The leucine and valine residues of the peptide are partly buried in two contiguous shallow, hydrophobic depressions. The anchoring phenylalanine is buried in a deep pocket formed by the aliphatic portions of two conserved arginine residues, along with an alanine and a proline, illustrating the unusual function of a cluster of basic residues in binding a hydrophobic motif.

Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3.,Miller GJ, Mattera R, Bonifacino JS, Hurley JH Nat Struct Biol. 2003 Aug;10(8):599-606. PMID:12858162<ref>PMID:12858162</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1p4u" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Bonifacino, J S]]

[[Category: Hurley, J H]]

[[Category: Mattera, R]]

[[Category: Miller, G J]]

[[Category: Protein transport]]