1gp0: Difference between revisions

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New page: left|200px<br /> <applet load="1gp0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gp0, resolution 1.40Å" /> '''HUMAN IGF2R DOMAIN ...
 
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[[Image:1gp0.gif|left|200px]]<br />
[[Image:1gp0.gif|left|200px]]<br /><applet load="1gp0" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1gp0" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1gp0, resolution 1.40&Aring;" />
caption="1gp0, resolution 1.40&Aring;" />
'''HUMAN IGF2R DOMAIN 11'''<br />
'''HUMAN IGF2R DOMAIN 11'''<br />


==Overview==
==Overview==
Insulin-like growth factor II receptor (IGF2R) is a multifunctional cell, surface receptor implicated in tumour suppression. Its growth inhibitory, activity has been associated with an ability to bind IGF-II. IGF2R, contains 15 homologous extracellular domains, with domain 11 primarily, responsible for IGF-II binding. We report a 1.4 A resolution crystal, structure of domain 11, solved using the anomalous scattering signal of, sulfur. The structure consists of two crossed beta-sheets forming a, flattened beta-barrel. Structural analysis identifies the putative IGF-II, binding site at one end of the beta-barrel whilst crystal lattice contacts, suggest a model for the full-length IGF2R extracellular region. The, structure factors and coordinates of IGF2R domain 11 have been deposited, in the Protein Data Bank (accession codes 1GP0 and 1GP3).
Insulin-like growth factor II receptor (IGF2R) is a multifunctional cell surface receptor implicated in tumour suppression. Its growth inhibitory activity has been associated with an ability to bind IGF-II. IGF2R contains 15 homologous extracellular domains, with domain 11 primarily responsible for IGF-II binding. We report a 1.4 A resolution crystal structure of domain 11, solved using the anomalous scattering signal of sulfur. The structure consists of two crossed beta-sheets forming a flattened beta-barrel. Structural analysis identifies the putative IGF-II binding site at one end of the beta-barrel whilst crystal lattice contacts suggest a model for the full-length IGF2R extracellular region. The structure factors and coordinates of IGF2R domain 11 have been deposited in the Protein Data Bank (accession codes 1GP0 and 1GP3).


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1GP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GP0 OCA].  
1GP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GP0 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brown, J.]]
[[Category: Brown, J.]]
[[Category: Esnouf, R.M.]]
[[Category: Esnouf, R M.]]
[[Category: Harlos, K.]]
[[Category: Harlos, K.]]
[[Category: Hassan, A.B.]]
[[Category: Hassan, A B.]]
[[Category: Jones, E.Y.]]
[[Category: Jones, E Y.]]
[[Category: Jones, M.A.]]
[[Category: Jones, M A.]]
[[Category: Linnell, J.]]
[[Category: Linnell, J.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: transport]]
[[Category: transport]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:07:40 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:27 2008''