1s4y
From Proteopedia
(New page: 200px<br /> <applet load="1s4y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s4y, resolution 2.30Å" /> '''Crystal structure o...) |
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| - | [[Image:1s4y.gif|left|200px]]<br /> | + | [[Image:1s4y.gif|left|200px]]<br /><applet load="1s4y" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1s4y, resolution 2.30Å" /> | caption="1s4y, resolution 2.30Å" /> | ||
'''Crystal structure of the activin/actrIIb extracellular domain'''<br /> | '''Crystal structure of the activin/actrIIb extracellular domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A new crystal structure of activin in complex with the extracellular | + | A new crystal structure of activin in complex with the extracellular domain of its type II receptor (ActRIIb-ECD) shows that the ligand exhibits an unexpected flexibility. The motion in the activin dimer disrupts its type I receptor interface, which may account for the disparity in its affinity for type I versus type II receptors. We have measured the affinities of activin and its antagonist inhibin for ActRIIb-ECD and found that the affinity of the 2-fold symmetric homodimer activin for ActRIIb-ECD depends on the availability of two spatially coupled ActRIIb-ECD molecules, whereas the affinity of the heterodimer inhibin does not. Our results indicate that activin's affinity for its two receptor types is greatly influenced by their membrane-restricted setting. We propose that activin affinity is modulated by the ligand flexibility and that cooperativity is achieved by binding to two ActRII chains that immobilize activin in a type I binding-competent orientation. |
==About this Structure== | ==About this Structure== | ||
| - | 1S4Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http:// | + | 1S4Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Allendorph, G | + | [[Category: Allendorph, G P.]] |
[[Category: Choe, S.]] | [[Category: Choe, S.]] | ||
| - | [[Category: Fischer, W | + | [[Category: Fischer, W H.]] |
[[Category: Greenwald, J.]] | [[Category: Greenwald, J.]] | ||
| - | [[Category: JCSG, Joint | + | [[Category: JCSG, Joint Center for Structural Genomics.]] |
[[Category: Vale, W.]] | [[Category: Vale, W.]] | ||
| - | [[Category: Vega, M | + | [[Category: Vega, M E.]] |
[[Category: jcsg]] | [[Category: jcsg]] | ||
[[Category: joint center for structural genomics]] | [[Category: joint center for structural genomics]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:00 2008'' |
Revision as of 12:58, 21 February 2008
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Crystal structure of the activin/actrIIb extracellular domain
Overview
A new crystal structure of activin in complex with the extracellular domain of its type II receptor (ActRIIb-ECD) shows that the ligand exhibits an unexpected flexibility. The motion in the activin dimer disrupts its type I receptor interface, which may account for the disparity in its affinity for type I versus type II receptors. We have measured the affinities of activin and its antagonist inhibin for ActRIIb-ECD and found that the affinity of the 2-fold symmetric homodimer activin for ActRIIb-ECD depends on the availability of two spatially coupled ActRIIb-ECD molecules, whereas the affinity of the heterodimer inhibin does not. Our results indicate that activin's affinity for its two receptor types is greatly influenced by their membrane-restricted setting. We propose that activin affinity is modulated by the ligand flexibility and that cooperativity is achieved by binding to two ActRII chains that immobilize activin in a type I binding-competent orientation.
About this Structure
1S4Y is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
A flexible activin explains the membrane-dependent cooperative assembly of TGF-beta family receptors., Greenwald J, Vega ME, Allendorph GP, Fischer WH, Vale W, Choe S, Mol Cell. 2004 Aug 13;15(3):485-9. PMID:15304227
Page seeded by OCA on Thu Feb 21 14:58:00 2008
Categories: Homo sapiens | Mus musculus | Non-specific serine/threonine protein kinase | Protein complex | Allendorph, G P. | Choe, S. | Fischer, W H. | Greenwald, J. | JCSG, Joint Center for Structural Genomics. | Vale, W. | Vega, M E. | Jcsg | Joint center for structural genomics | Protein structure initiative | Psi | Structural genomics | Transferase
