2cnj: Difference between revisions
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<StructureSection load='2cnj' size='340' side='right'caption='[[2cnj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2cnj' size='340' side='right'caption='[[2cnj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cnj]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2cnj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CNJ FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e6f|1e6f]], [[1gp0|1gp0]], [[1gp3|1gp3]], [[1gqb|1gqb]], [[1jpl|1jpl]], [[1jwg|1jwg]], [[1lf8|1lf8]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e6f|1e6f]], [[1gp0|1gp0]], [[1gp3|1gp3]], [[1gqb|1gqb]], [[1jpl|1jpl]], [[1jwg|1jwg]], [[1lf8|1lf8]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cnj OCA], [https://pdbe.org/2cnj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cnj RCSB], [https://www.ebi.ac.uk/pdbsum/2cnj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cnj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 09:59, 1 December 2021
NMR studies on the interaction of Insulin-Growth Factor II (IGF-II) with IGF2R domain 11NMR studies on the interaction of Insulin-Growth Factor II (IGF-II) with IGF2R domain 11
Structural highlights
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. Publication Abstract from PubMedThe insulin-like growth factor II/mannose-6-phosphate receptor (IGF2R) mediates trafficking of mannose-6-phosphate (M6P)-containing proteins and the mitogenic hormone IGF2. IGF2R also plays an important role as a tumor suppressor, as mutation is frequently associated with human carcinogenesis. IGF2 binds to domain 11, one of 15 extracellular domains on IGF2R. The crystal structure of domain 11 and the solution structure of IGF2 have been reported, but, to date, there has been limited success when using crystallography to study the interaction of IGFs with their binding partners. As an approach to investigate the interaction between IGF2 and IGF2R, we have used heteronuclear NMR in combination with existing mutagenesis data to derive models of the domain 11-IGF2 complex by using the program HADDOCK. The models reveal that the molecular interaction is driven by critical hydrophobic residues on IGF2 and IGF2R, while a ring of flexible, charged residues on IGF2R may modulate binding. Structural insights into the interaction of insulin-like growth factor 2 with IGF2R domain 11.,Williams C, Rezgui D, Prince SN, Zaccheo OJ, Foulstone EJ, Forbes BE, Norton RS, Crosby J, Hassan AB, Crump MP Structure. 2007 Sep;15(9):1065-78. PMID:17850746[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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