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1gyv

From Proteopedia

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

Structural highlights

1gyv is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.71Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kent HM, McMahon HT, Evans PR, Benmerah A, Owen DJ. Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin. Structure. 2002 Aug;10(8):1139-48. PMID:12176391

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gyv"

@@ Line 3: / Line 3: @@
 <StructureSection load='1gyv' size='340' side='right'caption='[[1gyv]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gyv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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>
+<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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gyu|1gyu]], [[1gyw|1gyw]]</div></td></tr>
+</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>
 <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>
 </table>
+== Function ==
+[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Evans, P R]]
+[[Category: Evans PR]]
-[[Category: Kent, H M]]
+[[Category: Kent HM]]
-[[Category: McMahon, H M]]
+[[Category: McMahon HM]]
-[[Category: Owen, D J]]
+[[Category: Owen DJ]]
-[[Category: Adaptin]]
-[[Category: Adaptor]]
-[[Category: Clathrin]]
-[[Category: Endocytosis]]
-[[Category: Golgi]]

1gyv

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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