1s4y

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{{STRUCTURE_1s4y| PDB=1s4y | SCENE= }}
{{STRUCTURE_1s4y| PDB=1s4y | SCENE= }}
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'''Crystal structure of the activin/actrIIb extracellular domain'''
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===Crystal structure of the activin/actrIIb extracellular domain===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15304227 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15304227}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:18:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:44:10 2008''

Revision as of 17:44, 28 July 2008

Image:1s4y.png

Template:STRUCTURE 1s4y

Crystal structure of the activin/actrIIb extracellular domain

Template:ABSTRACT PUBMED 15304227

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

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