This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2arv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2arv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2arv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2arv| PDB=2arv | SCENE= }}
{{STRUCTURE_2arv| PDB=2arv | SCENE= }}
-
'''Structure of human Activin A'''
+
===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.
+
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.
 +
-->
 +
{{ABSTRACT_PUBMED_16482217}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Disulfide linked]]
[[Category: Disulfide linked]]
[[Category: Homodimer,cystine knot]]
[[Category: Homodimer,cystine knot]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:24:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:25:47 2008''

Revision as of 01:25, 28 July 2008

Image:2arv.png

Template:STRUCTURE 2arv

Structure of human Activin A

Template:ABSTRACT PUBMED 16482217

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 Jul 28 04:25:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2arv"
Personal tools