1mhq

From Proteopedia

(Difference between revisions)

Revision as of 08:54, 21 April 2021

Crystal Structure Of Human GGA2 VHS Domain

Structural highlights

1mhq is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GGA2_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.

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

Golgi-localized, gamma-ear-containing, ARF binding (GGA) proteins regulate intracellular vesicle transport by recognizing sorting signals on the cargo surface in the initial step of the budding process. The VHS (VPS27, Hrs, and STAM) domain of GGA binds with the signal peptides. Here, a crystal structure of the VHS domain of GGA2 is reported at 2.2 A resolution, which permits a direct comparison with that of homologous proteins, GGA1 and GGA3. Significant structural difference is present in the loop between helices 6 and 7, which forms part of the ligand binding pocket. Intrinsic fluorescence spectroscopic study indicates that this loop undergoes a conformational change upon ligand binding. Thus, the current structure suggests that a conformational change induced by ligand binding occurs in this part of the ligand pocket.

Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket.,Zhu G, He X, Zhai P, Terzyan S, Tang J, Zhang XC FEBS Lett. 2003 Feb 27;537(1-3):171-6. PMID:12606052^[1]

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

References

↑ Zhu G, He X, Zhai P, Terzyan S, Tang J, Zhang XC. Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket. FEBS Lett. 2003 Feb 27;537(1-3):171-6. PMID:12606052

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1mhq' size='340' side='right'caption='[[1mhq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mhq]] 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=1MHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MHQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mhq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MHQ FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhq OCA], [http://pdbe.org/1mhq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mhq RCSB], [http://www.ebi.ac.uk/pdbsum/1mhq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mhq ProSAT]</span></td></tr>
+</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=1mhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhq OCA], [https://pdbe.org/1mhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mhq RCSB], [https://www.ebi.ac.uk/pdbsum/1mhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mhq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GGA2_HUMAN GGA2_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.
+[[https://www.uniprot.org/uniprot/GGA2_HUMAN GGA2_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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1mhq

From Proteopedia

Revision as of 08:54, 21 April 2021

Crystal Structure Of Human GGA2 VHS Domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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