2arp: Difference between revisions
New page: left|200px<br /> <applet load="2arp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2arp, resolution 2.00Å" /> '''Activin A in comple... |
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[[Image:2arp.gif|left|200px]]<br /> | [[Image:2arp.gif|left|200px]]<br /><applet load="2arp" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2arp" size=" | |||
caption="2arp, resolution 2.00Å" /> | caption="2arp, resolution 2.00Å" /> | ||
'''Activin A in complex with Fs12 fragment of follistatin'''<br /> | '''Activin A in complex with Fs12 fragment of follistatin'''<br /> | ||
==Overview== | ==Overview== | ||
The secreted, multidomain protein follistatin binds activins with high | 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. | ||
==About this Structure== | ==About this Structure== | ||
2ARP 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/Rattus_norvegicus Rattus norvegicus] with NI, 1PG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2ARP 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/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=1PG:'>1PG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Harrington, A | [[Category: Harrington, A E.]] | ||
[[Category: Hyvonen, M.]] | [[Category: Hyvonen, M.]] | ||
[[Category: Morris-Triggs, S | [[Category: Morris-Triggs, S A.]] | ||
[[Category: Ohnuma, S.]] | [[Category: Ohnuma, S.]] | ||
[[Category: Robinson, C | [[Category: Robinson, C V.]] | ||
[[Category: Ruotolo, B | [[Category: Ruotolo, B T.]] | ||
[[Category: 1PG]] | [[Category: 1PG]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: protein complex]] | [[Category: protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:16 2008'' | ||
Revision as of 17:30, 21 February 2008
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Activin A in complex with Fs12 fragment of follistatin
OverviewOverview
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.
About this StructureAbout this Structure
2ARP is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the inhibition of activin signalling by follistatin., Harrington AE, Morris-Triggs SA, Ruotolo BT, Robinson CV, Ohnuma S, Hyvonen M, EMBO J. 2006 Mar 8;25(5):1035-45. Epub 2006 Feb 16. PMID:16482217
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