1s4y

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[[Image:1s4y.gif|left|200px]]
[[Image:1s4y.gif|left|200px]]
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{{Structure
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|PDB= 1s4y |SIZE=350|CAPTION= <scene name='initialview01'>1s4y</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1s4y", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE= ACVR2B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), INHBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01064 Activin_recp], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00019 TGF_beta]</span>
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{{STRUCTURE_1s4y| PDB=1s4y | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4y OCA], [http://www.ebi.ac.uk/pdbsum/1s4y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s4y RCSB]</span>
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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.]]
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[[Category: Vega, M E.]]
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[[Category: joint center for structural genomic]]
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[[Category: Joint center for structural genomic]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomic]]
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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 Sun Mar 30 23:37:23 2008''
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Revision as of 05:18, 3 May 2008

Template:STRUCTURE 1s4y

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

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