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| {{STRUCTURE_2arp| PDB=2arp | SCENE= }} | | {{STRUCTURE_2arp| PDB=2arp | SCENE= }} |
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| '''Activin A in complex with Fs12 fragment of follistatin'''
| | ===Activin A in complex with Fs12 fragment of follistatin=== |
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| ==Overview==
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| The secreted, multidomain protein follistatin binds activins with high affinity, inhibiting their receptor interaction. We have dissected follistatin's domain structure and shown that the minimal activin-inhibiting fragment of follistatin is comprised of the first and second Fs domains (Fs12). This protein can bind to activin dimer and form a stable complex containing two Fs12 molecules and one activin dimer. We have solved crystal structures of activin A alone and its complex with Fs12 fragment to 2 A resolution. The complex structure shows how Fs12 molecules wrap around the back of the 'wings' of activin, blocking the type II receptor-binding site on activin A. Arginine 192 in Fs2 is a key residue in this interaction, inserting itself in between activin's fingers. Complex formation imposes a novel orientation for the EGF- and Kazal-like subdomains in the Fs2 domain and activin A shows further variation from the canonical TGF-beta family fold. The structure provides a detailed description of the inhibitory mechanism and gives insights into interactions of follistatin with other TGF-beta family proteins. | | The line below this paragraph, {{ABSTRACT_PUBMED_16482217}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16482217 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16482217}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Kazal domain]] | | [[Category: Kazal domain]] |
| [[Category: Protein complex]] | | [[Category: Protein complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:23:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:06:15 2008'' |
