2v5p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:31, 17 October 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2v5p.jpg|left|200px]]
 
-
{{Structure
+
==COMPLEX STRUCTURE OF HUMAN IGF2R DOMAINS 11-13 BOUND TO IGF-II==
-
|PDB= 2v5p |SIZE=350|CAPTION= <scene name='initialview01'>2v5p</scene>, resolution 4.10&Aring;
+
<StructureSection load='2v5p' size='340' side='right'caption='[[2v5p]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Nag+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC5:Bma+Binding+Site+For+Chain+A'>AC5</scene>, <scene name='pdbsite=AC6:Nag+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:Nag+Binding+Site+For+Chain+B'>AC7</scene> and <scene name='pdbsite=AC8:Bma+Binding+Site+For+Chain+A'>AC8</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
+
<table><tr><td colspan='2'>[[2v5p]] is a 4 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=2V5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5P FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2v5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5p OCA], [https://pdbe.org/2v5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5p RCSB], [https://www.ebi.ac.uk/pdbsum/2v5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5p 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/v5/2v5p_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2v5p ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Embryonic development and normal growth require exquisite control of insulin-like growth factors (IGFs). In mammals the extracellular region of the cation-independent mannose-6-phosphate receptor has gained an IGF-II-binding function and is termed type II IGF receptor (IGF2R). IGF2R sequesters IGF-II; imbalances occur in cancers and IGF2R is implicated in tumour suppression. We report crystal structures of IGF2R domains 11-12, 11-12-13-14 and domains 11-12-13/IGF-II complex. A distinctive juxtaposition of these domains provides the IGF-II-binding unit, with domain 11 directly interacting with IGF-II and domain 13 modulating binding site flexibility. Our complex shows that Phe19 and Leu53 of IGF-II lock into a hydrophobic pocket unique to domain 11 of mammalian IGF2Rs. Mutagenesis analyses confirm this IGF-II 'binding-hotspot', revealing that IGF-binding proteins and IGF2R have converged on the same high-affinity site.
-
'''COMPLEX STRUCTURE OF HUMAN IGF2R DOMAINS 11-13 BOUND TO IGF-II'''
+
Structure and functional analysis of the IGF-II/IGF2R interaction.,Brown J, Delaine C, Zaccheo OJ, Siebold C, Gilbert RJ, van Boxel G, Denley A, Wallace JC, Hassan AB, Forbes BE, Jones EY EMBO J. 2008 Jan 9;27(1):265-76. Epub 2007 Nov 29. PMID:18046459<ref>PMID:18046459</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2v5p" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Embryonic development and normal growth require exquisite control of insulin-like growth factors (IGFs). In mammals the extracellular region of the cation-independent mannose-6-phosphate receptor has gained an IGF-II-binding function and is termed type II IGF receptor (IGF2R). IGF2R sequesters IGF-II; imbalances occur in cancers and IGF2R is implicated in tumour suppression. We report crystal structures of IGF2R domains 11-12, 11-12-13-14 and domains 11-12-13/IGF-II complex. A distinctive juxtaposition of these domains provides the IGF-II-binding unit, with domain 11 directly interacting with IGF-II and domain 13 modulating binding site flexibility. Our complex shows that Phe19 and Leu53 of IGF-II lock into a hydrophobic pocket unique to domain 11 of mammalian IGF2Rs. Mutagenesis analyses confirm this IGF-II 'binding-hotspot', revealing that IGF-binding proteins and IGF2R have converged on the same high-affinity site.
+
*[[Insulin-like growth factor receptor|Insulin-like growth factor receptor]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
2V5P is a [[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=2V5P OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Structure and functional analysis of the IGF-II/IGF2R interaction., Brown J, Delaine C, Zaccheo OJ, Siebold C, Gilbert RJ, van Boxel G, Denley A, Wallace JC, Hassan AB, Forbes BE, Jones EY, EMBO J. 2008 Jan 9;27(1):265-76. Epub 2007 Nov 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18046459 18046459]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Boxel, G Van.]]
+
[[Category: Brown J]]
-
[[Category: Brown, J.]]
+
[[Category: Delaine C]]
-
[[Category: Delaine, C.]]
+
[[Category: Denley A]]
-
[[Category: Denley, A.]]
+
[[Category: Forbes BE]]
-
[[Category: Forbes, B E.]]
+
[[Category: Gilbert RJ]]
-
[[Category: Gilbert, R J.]]
+
[[Category: Hassan AB]]
-
[[Category: Hassan, A B.]]
+
[[Category: Jones EY]]
-
[[Category: Jones, E Y.]]
+
[[Category: Siebold C]]
-
[[Category: Siebold, C.]]
+
[[Category: Wallace JC]]
-
[[Category: Wallace, J C.]]
+
[[Category: Zaccheo OJ]]
-
[[Category: Zaccheo, O J.]]
+
[[Category: Van Boxel G]]
-
[[Category: NAG]]
+
-
[[Category: beta barrel]]
+
-
[[Category: cation independent mannose 6-phosphate]]
+
-
[[Category: fibronectin type ii]]
+
-
[[Category: glycoprotein]]
+
-
[[Category: insulin-like growth factor]]
+
-
[[Category: lysosome]]
+
-
[[Category: membrane]]
+
-
[[Category: phosphorylation]]
+
-
[[Category: polymorphism]]
+
-
[[Category: receptor]]
+
-
[[Category: receptor/glycoprotein complex]]
+
-
[[Category: transmembrane]]
+
-
[[Category: transport]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:16 2008''
+

Current revision

COMPLEX STRUCTURE OF HUMAN IGF2R DOMAINS 11-13 BOUND TO IGF-II

PDB ID 2v5p

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v5p"
Personal tools