2arv
From Proteopedia
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|PDB= 2arv |SIZE=350|CAPTION= <scene name='initialview01'>2arv</scene>, resolution 2.00Å | |PDB= 2arv |SIZE=350|CAPTION= <scene name='initialview01'>2arv</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= INHBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= INHBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2arp|2ARP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2arv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2arv OCA], [http://www.ebi.ac.uk/pdbsum/2arv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2arv RCSB]</span> | ||
}} | }} | ||
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[[Category: Robinson, C V.]] | [[Category: Robinson, C V.]] | ||
[[Category: Ruotolo, B T.]] | [[Category: Ruotolo, B T.]] | ||
| - | [[Category: 1PG]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: cystine knot]] | ||
[[Category: disulfide linked]] | [[Category: disulfide linked]] | ||
| - | [[Category: homodimer]] | + | [[Category: homodimer,cystine knot]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:56:27 2008'' |
Revision as of 22:56, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | INHBA (Homo sapiens) | ||||||
| Related: | 2ARP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 01:56:27 2008
