1jpl: Difference between revisions

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-[[Image:1jpl.jpg|left|200px]]<br /><applet load="1jpl" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1jpl, resolution 2.40&Aring;" />
-'''GGA3 VHS domain complexed with C-terminal peptide from cation-independent mannose 6-phosphate receptor'''<br />
-==Overview==
+==GGA3 VHS domain complexed with C-terminal peptide from cation-independent mannose 6-phosphate receptor==
-Specific sorting signals direct transmembrane proteins to the compartments, of the endosomal-lysosomal system. Acidic-cluster-dileucine signals, present within the cytoplasmic tails of sorting receptors, such as the, cation-independent and cation-dependent mannose-6-phosphate receptors, are, recognized by the GGA (Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding) proteins. The VHS (Vps27p, Hrs and STAM), domains of the GGA proteins are responsible for the highly specific, recognition of these acidic-cluster-dileucine signals. Here we report the, structures of the VHS domain of human GGA3 complexed with signals from, both mannose-6-phosphate receptors. The signals bind in an extended, conformation to helices 6 and 8 of the VHS domain. The structures, highlight an Asp residue separated by two residues from a dileucine, sequence as critical recognition elements. The side chains of the, Asp-X-X-Leu-Leu sequence interact with subsites consisting of one, electropositive and two shallow hydrophobic pockets, respectively. The, rigid spatial alignment of the three binding subsites leads to high, specificity.
+<StructureSection load='1jpl' size='340' side='right'caption='[[1jpl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
-==Disease==
+<table><tr><td colspan='2'>[[1jpl]] is a 8 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=1JPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JPL FirstGlance]. <br>
-Known diseases associated with this structure: Hepatocellular carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147280 147280]]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-==About this Structure==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jpl OCA], [https://pdbe.org/1jpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jpl RCSB], [https://www.ebi.ac.uk/pdbsum/1jpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jpl ProSAT]</span></td></tr>
-JPL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1JPL OCA].
+</table>
+== Function ==
-==Reference==
+[https://www.uniprot.org/uniprot/MPRI_HUMAN MPRI_HUMAN] Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation, by binding DPP4.<ref>PMID:10900005</ref>
-Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains., Misra S, Puertollano R, Kato Y, Bonifacino JS, Hurley JH, Nature. 2002 Feb 21;415(6874):933-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11859375 11859375]
+== 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/jp/1jpl_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=1jpl ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Bonifacino, J.S.]]
+[[Category: Bonifacino JS]]
-[[Category: Hurley, J.H.]]
+[[Category: Hurley JH]]
-[[Category: Misra, S.]]
+[[Category: Misra S]]
-[[Category: Puertollano, R.]]
+[[Category: Puertollano R]]
-[[Category: protein-peptide complex; vhs domain; dxxll sorting signal]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:08:31 2008''