2v5p: Difference between revisions

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[[Image:2v5p.~~jpg~~|left|200px]]

[[Image:2v5p.png|left|200px]]

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

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

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_18046459}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18046459 is the PubMed ID number.

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==About this Structure==

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[[Category: Transmembrane]]

[[Category: Transport]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Apr 24 09~~:30:17 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:17:33 2008''

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-[[Image:2v5p.jpg|left|200px]]
+{{Seed}}
+[[Image:2v5p.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2v5p|  PDB=2v5p  |  SCENE=  }}
-'''COMPLEX STRUCTURE OF HUMAN IGF2R DOMAINS 11-13 BOUND TO IGF-II'''
+===COMPLEX STRUCTURE OF HUMAN IGF2R DOMAINS 11-13 BOUND TO IGF-II===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18046459}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18046459 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18046459}}
 ==About this Structure==
@@ Line 46: / Line 50: @@
 [[Category: Transmembrane]]
 [[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:30:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:17:33 2008''