2goo: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:2goo.gif|left|200px]]
{{Seed}}
[[Image:2goo.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2goo|  PDB=2goo  |  SCENE=  }}  
{{STRUCTURE_2goo|  PDB=2goo  |  SCENE=  }}  


'''Ternary Complex of BMP-2 bound to BMPR-Ia-ECD and ActRII-ECD'''
===Ternary Complex of BMP-2 bound to BMPR-Ia-ECD and ActRII-ECD===




==Overview==
<!--
The crystal structure of the complete signaling complex formed between bone morphogenetic protein 2 (BMP-2) and the extracellular domains (ECDs) of its type I receptor [bone morphogenetic protein receptor type Ia (BMPR-Ia)-ECD] and its type II receptor [activin receptor type II (ActRII)-ECD] shows two fundamental structural constraints for receptor assembly. First, the homodimeric BMP-2 ligand assembles two pairs of each receptor symmetrically, where each of the receptor ECDs does not make physical contact. Therefore, conformational communication between receptor ECDs, if any, should be propagated through the central ligand. Second, the type I and II receptor interfaces of the complex, when compared with those of binary complexes such as BMP-2/BMPR Ia-ECD, BMP-7/ActRII-ECD, and activin/ActRIIb-ECD, respectively, show there are common sets of positions repeatedly used by both ligands and receptors. Therefore, specificity-determining amino acid differences at the receptor interfaces should also account for the disparity in affinity of individual receptors for different ligand subunits. We find that a specific mutation to BMP-2 increases its affinity to ActRII-ECD by 5-fold. These results together establish that the specific signaling output is largely determined by two variables, the ligand-receptor pair identity and the mode of cooperative assembly of relevant receptors governed by the ligand flexibility in a membrane-restricted manner.
The line below this paragraph, {{ABSTRACT_PUBMED_16672363}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16672363 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16672363}}


==Disease==
==Disease==
Line 34: Line 38:
[[Category: Bmpr-ia]]
[[Category: Bmpr-ia]]
[[Category: Tgf-beta]]
[[Category: Tgf-beta]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:20:43 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:15:28 2008''

Revision as of 08:15, 28 July 2008

File:2goo.png

Template:STRUCTURE 2goo

Ternary Complex of BMP-2 bound to BMPR-Ia-ECD and ActRII-ECD

Template:ABSTRACT PUBMED 16672363

Disease

Known disease associated with this structure: HFE hemochromatosis, modifier of OMIM:[112261], Juvenile polyposis syndrome, infantile form OMIM:[601299], Polyposis syndrome, hereditary mixed, 2 OMIM:[601299], Polyposis, juvenile intestinal OMIM:[601299]

About this Structure

2GOO is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of the ternary signaling complex of a TGF-beta superfamily member., Allendorph GP, Vale WW, Choe S, Proc Natl Acad Sci U S A. 2006 May 16;103(20):7643-8. Epub 2006 May 3. PMID:16672363

Page seeded by OCA on Mon Jul 28 11:15:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2goo&oldid=695904"