2arv
From Proteopedia
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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 SO4, 1PG and GOL 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
Page seeded by OCA on Mon Nov 12 20:54:03 2007
