1s4y
From Proteopedia
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'''Crystal structure of the activin/actrIIb extracellular domain''' | '''Crystal structure of the activin/actrIIb extracellular domain''' | ||
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[[Category: Vale, W.]] | [[Category: Vale, W.]] | ||
[[Category: Vega, M E.]] | [[Category: Vega, M E.]] | ||
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| - | [[Category: | + | [[Category: Joint center for structural genomic]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:18:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:18, 3 May 2008
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. 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 Sat May 3 08:18:17 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 genomic | Protein structure initiative | Psi | Structural genomic | Transferase
