2arv
From Proteopedia
(New page: 200px<br /> <applet load="2arv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2arv, resolution 2.00Å" /> '''Structure of human ...) |
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| - | [[Image:2arv.gif|left|200px]]<br /> | + | [[Image:2arv.gif|left|200px]]<br /><applet load="2arv" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2arv" size=" | + | |
caption="2arv, resolution 2.00Å" /> | caption="2arv, resolution 2.00Å" /> | ||
'''Structure of human Activin A'''<br /> | '''Structure of human Activin A'''<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== | ||
| - | 2ARV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4, 1PG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2ARV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</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=2ARV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[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: homodimer]] | [[Category: homodimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:23 2008'' |
Revision as of 14:30, 21 February 2008
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Structure of human Activin A
Overview
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
2ARV is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
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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