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1e6f

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[[Image:1e6f.gif|left|200px]]
 
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{{Structure
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==Human MIR-receptor, repeat 11==
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|PDB= 1e6f |SIZE=350|CAPTION= <scene name='initialview01'>1e6f</scene>, resolution 1.75&Aring;
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<StructureSection load='1e6f' size='340' side='right'caption='[[1e6f]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1e6f]] is a 2 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=1E6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E6F 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]] 1.75&#8491;</td></tr>
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|GENE=
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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=1e6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6f OCA], [https://pdbe.org/1e6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e6f RCSB], [https://www.ebi.ac.uk/pdbsum/1e6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e6f ProSAT]</span></td></tr>
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}}
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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/e6/1e6f_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=1e6f ConSurf].
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<div style="clear:both"></div>
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'''HUMAN MIR-RECEPTOR, REPEAT 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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Improved data quality now makes it feasible to exploit the weak anomalous signal derived only from the sulfurs inherent to the protein or in particular from halide ions incorporated by soaking. The latter technique requires the location of a high number of partially occupied halide sites. This number appears to be roughly proportional to the exposed protein surface. This paper explores the application of dual-space ab initio methods as implemented in the program SHELXD to the location of substructures of sulfur in SAD experiments, bromide in SAD and MAD experiments and iodide using SAD and SIRAS to determine the anomalous-atom substructure. Sets of atoms consistent with the Patterson function were generated as a starting point for the dual-space recycling procedure in SHELXD. The substructure is then expanded to the full structure by maximum-likelihood phasing with SHARP and density modification with the program DM. Success in the location of the substructures and subsequent phasing depends critically on the quality of the data and on the extent of the anomalous signal. This varies with each crystal and soak, but for the same crystal the significance of the anomalous signal was found to be highly sensitive to the redundancy of the intensity measurements, which in some cases made all the difference. This is illustrated by the determination of the previously unknown structure of repeat 11 of the human mannose-6-phosphate/insulin-like growth factor II receptor (Man6P/IGFII-receptor), with 310 amino acids in the asymmetric unit, which was phased by soaking the crystals in a cryoprotectant solution containing halide anions.
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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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1E6F 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=1E6F OCA].
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==Reference==
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Locating the anomalous scatterer substructures in halide and sulfur phasing., Uson I, Schmidt B, von Bulow R, Grimme S, von Figura K, Dauter M, Rajashankar KR, Dauter Z, Sheldrick GM, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):57-66. Epub 2002, Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12499540 12499540]
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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: Buelow, R Von.]]
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[[Category: Dauter M]]
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[[Category: Dauter, M.]]
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[[Category: Dauter Z]]
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[[Category: Dauter, Z.]]
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[[Category: Grimme S]]
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[[Category: Figura, K Von.]]
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[[Category: Rajashankar KR]]
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[[Category: Grimme, S.]]
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[[Category: Schmidt B]]
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[[Category: Rajashankar, K R.]]
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[[Category: Uson I]]
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[[Category: Schmidt, B.]]
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[[Category: Von Buelow R]]
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[[Category: Uson, I.]]
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[[Category: Von Figura K]]
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[[Category: glycoprotein]]
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[[Category: igf-ii receptor]]
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[[Category: mir-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 10:50:30 2008''
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Current revision

Human MIR-receptor, repeat 11

PDB ID 1e6f

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