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2v5p

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(New page: 200px<br /><applet load="2v5p" size="350" color="white" frame="true" align="right" spinBox="true" caption="2v5p, resolution 4.10&Aring;" /> '''COMPLEX STRUCTURE OF...)
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==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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2V5P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5P OCA].
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2V5P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5P OCA].
==Reference==
==Reference==
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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. 2007 Nov 29;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18046459 18046459]
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18046459 18046459]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Boxel, G.Van.]]
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[[Category: Boxel, G Van.]]
[[Category: Brown, J.]]
[[Category: Brown, J.]]
[[Category: Delaine, C.]]
[[Category: Delaine, C.]]
[[Category: Denley, A.]]
[[Category: Denley, A.]]
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[[Category: Forbes, B.E.]]
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[[Category: Forbes, B E.]]
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[[Category: Gilbert, R.J.]]
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[[Category: Gilbert, R J.]]
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[[Category: Hassan, A.B.]]
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[[Category: Hassan, A B.]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones, E Y.]]
[[Category: Siebold, C.]]
[[Category: Siebold, C.]]
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[[Category: Wallace, J.C.]]
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[[Category: Wallace, J C.]]
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[[Category: Zaccheo, O.J.]]
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[[Category: Zaccheo, O J.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: beta barrel]]
[[Category: beta barrel]]
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[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:46:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:53:20 2008''

Revision as of 16:53, 21 February 2008


2v5p, resolution 4.10Å

Drag the structure with the mouse to rotate

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.

About this Structure

2V5P is a Protein complex structure of sequences from Homo sapiens with as ligand. Known structural/functional Sites: , , , , , and . Full crystallographic information is available from OCA.

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:18046459

Page seeded by OCA on Thu Feb 21 18:53:20 2008

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