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1gp0

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[[Image:1gp0.gif|left|200px]]
 
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{{Structure
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==Human IGF2R domain 11==
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|PDB= 1gp0 |SIZE=350|CAPTION= <scene name='initialview01'>1gp0</scene>, resolution 1.40&Aring;
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<StructureSection load='1gp0' size='340' side='right'caption='[[1gp0]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1gp0]] 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=1GP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GP0 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp0 OCA], [https://pdbe.org/1gp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gp0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gp0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/1gp0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1gp0 ConSurf].
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<div style="clear:both"></div>
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'''HUMAN IGF2R DOMAIN 11'''
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==See Also==
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*[[Insulin-like growth factor receptor|Insulin-like growth factor receptor]]
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== References ==
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==Overview==
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<references/>
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Insulin-like growth factor II receptor (IGF2R) is a multifunctional cell surface receptor implicated in tumour suppression. Its growth inhibitory activity has been associated with an ability to bind IGF-II. IGF2R contains 15 homologous extracellular domains, with domain 11 primarily responsible for IGF-II binding. We report a 1.4 A resolution crystal structure of domain 11, solved using the anomalous scattering signal of sulfur. The structure consists of two crossed beta-sheets forming a flattened beta-barrel. Structural analysis identifies the putative IGF-II binding site at one end of the beta-barrel whilst crystal lattice contacts suggest a model for the full-length IGF2R extracellular region. The structure factors and coordinates of IGF2R domain 11 have been deposited in the Protein Data Bank (accession codes 1GP0 and 1GP3).
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__TOC__
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</StructureSection>
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==Disease==
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Known diseases associated with this structure: Hepatocellular carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147280 147280]]
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==About this Structure==
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1GP0 is a [[Single protein]] structure of sequence 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=1GP0 OCA].
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==Reference==
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Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur., Brown J, Esnouf RM, Jones MA, Linnell J, Harlos K, Hassan AB, Jones EY, EMBO J. 2002 Mar 1;21(5):1054-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11867533 11867533]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brown, J.]]
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[[Category: Brown J]]
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[[Category: Esnouf, R M.]]
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[[Category: Esnouf RM]]
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[[Category: Harlos, K.]]
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[[Category: Harlos K]]
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[[Category: Hassan, A B.]]
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[[Category: Hassan AB]]
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[[Category: Jones, E Y.]]
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[[Category: Jones EY]]
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[[Category: Jones, M A.]]
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[[Category: Jones MA]]
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[[Category: Linnell, J.]]
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[[Category: Linnell J]]
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[[Category: SO4]]
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[[Category: beta barrel]]
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[[Category: cation independent mannose 6-phosphate]]
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[[Category: insulin-like growth factor]]
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[[Category: receptor]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:03 2008''
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Current revision

Human IGF2R domain 11

PDB ID 1gp0

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