1gp0: Difference between revisions

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New page: left|200px<br /> <applet load="1gp0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gp0, resolution 1.40Å" /> '''HUMAN IGF2R DOMAIN ...
 
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[[Image:1gp0.gif|left|200px]]<br />
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'''HUMAN IGF2R DOMAIN 11'''<br />


==Overview==
==Human IGF2R domain 11==
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).
<StructureSection load='1gp0' size='340' side='right'caption='[[1gp0]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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>
== 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/gp/1gp0_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=1gp0 ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Hepatocellular carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147280 147280]]
*[[Insulin-like growth factor receptor|Insulin-like growth factor receptor]]
 
== References ==
==About this Structure==
<references/>
1GP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GP0 OCA].
__TOC__
 
</StructureSection>
==Reference==
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11867533 11867533]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brown, J.]]
[[Category: Brown J]]
[[Category: Esnouf, R.M.]]
[[Category: Esnouf RM]]
[[Category: Harlos, K.]]
[[Category: Harlos K]]
[[Category: Hassan, A.B.]]
[[Category: Hassan AB]]
[[Category: Jones, E.Y.]]
[[Category: Jones EY]]
[[Category: Jones, M.A.]]
[[Category: Jones MA]]
[[Category: Linnell, J.]]
[[Category: Linnell J]]
[[Category: SO4]]
[[Category: beta barrel]]
[[Category: cation independent mannose 6-phosphate]]
[[Category: insulin-like growth factor]]
[[Category: receptor]]
[[Category: transport]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:07:40 2007''

Latest revision as of 14:23, 27 March 2024

Human IGF2R domain 11Human IGF2R domain 11

Structural highlights

1gp0 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Ikushima H, Munakata Y, Ishii T, Iwata S, Terashima M, Tanaka H, Schlossman SF, Morimoto C. Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8439-44. PMID:10900005

1gp0, resolution 1.40Å

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