2v5o: Difference between revisions
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[[Image:2v5o.jpg|left|200px]] | [[Image:2v5o.jpg|left|200px]] | ||
'''STRUCTURE OF HUMAN IGF2R DOMAINS 11-14''' | {{Structure | ||
|PDB= 2v5o |SIZE=350|CAPTION= <scene name='initialview01'>2v5o</scene>, resolution 2.91Å | |||
|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=AC4:Cl+Binding+Site+For+Chain+A'>AC4</scene> and <scene name='pdbsite=AC5:Cl+Binding+Site+For+Chain+A'>AC5</scene> | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF HUMAN IGF2R DOMAINS 11-14''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2V5O is a [ | 2V5O is a [[Single protein]] structure of sequence 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=2V5O OCA]. | ||
==Reference== | ==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:// | 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: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:25 2008'' | ||
Revision as of 16:43, 20 March 2008
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| 2v5o, resolution 2.91Å | |||||||||||||
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| Sites: | AC1, AC2, AC3, AC4 and AC5 | ||||||||||||
| Ligands: | NAG and CL | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF HUMAN IGF2R DOMAINS 11-14
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
2V5O is a Single protein structure of sequence from Homo sapiens. 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 Mar 20 18:43:25 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Homo sapiens
- Single protein
- Boxel, G Van.
- Brown, J.
- Delaine, C.
- Denley, A.
- Forbes, B E.
- Gilbert, R J.
- Hassan, A B.
- Jones, E Y.
- Siebold, C.
- Wallace, J C.
- Zaccheo, O J.
- CL
- NAG
- Beta barrel
- Cation independent mannose 6-phosphate
- Fibronectin type ii
- Glycoprotein
- Insulin-like growth factor
- Lysosome
- Membrane
- Phosphorylation
- Polymorphism
- Receptor
- Transmembrane
- Transport