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1nys

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[[Image:1nys.gif|left|200px]]<br /><applet load="1nys" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nys.gif|left|200px]]
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caption="1nys, resolution 3.05&Aring;" />
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'''Crystal Structure of Activin A Bound to the ECD of ActRIIB P41'''<br />
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{{Structure
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|PDB= 1nys |SIZE=350|CAPTION= <scene name='initialview01'>1nys</scene>, resolution 3.05&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= actrIIb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), INHBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of Activin A Bound to the ECD of ActRIIB P41'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NYS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYS OCA].
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1NYS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYS OCA].
==Reference==
==Reference==
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Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions., Thompson TB, Woodruff TK, Jardetzky TS, EMBO J. 2003 Apr 1;22(7):1555-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12660162 12660162]
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Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions., Thompson TB, Woodruff TK, Jardetzky TS, EMBO J. 2003 Apr 1;22(7):1555-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12660162 12660162]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: type ii]]
[[Category: type ii]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:03:31 2008''

Revision as of 11:03, 20 March 2008


PDB ID 1nys

Drag the structure with the mouse to rotate
, resolution 3.05Å
Gene: actrIIb (Rattus norvegicus), INHBA (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Activin A Bound to the ECD of ActRIIB P41


Overview

The TGF-beta superfamily of ligands and receptors stimulate cellular events in diverse processes ranging from cell fate specification in development to immune suppression. Activins define a major subgroup of TGF-beta ligands that regulate cellular differentiation, proliferation, activation and apoptosis. Activins signal through complexes formed with type I and type II serine/threonine kinase receptors. We have solved the crystal structure of activin A bound to the extracellular domain of a type II receptor, ActRIIB, revealing the details of this interaction. ActRIIB binds to the outer edges of the activin finger regions, with the two receptors juxtaposed in close proximity, in a mode that differs from TGF-beta3 binding to type II receptors. The dimeric activin A structure differs from other known TGF-beta ligand structures, adopting a compact folded-back conformation. The crystal structure of the complex is consistent with recruitment of two type I receptors into a close packed arrangement at the cell surface and suggests that diversity in the conformational arrangements of TGF-beta ligand dimers could influence cellular signaling processes.

About this Structure

1NYS is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions., Thompson TB, Woodruff TK, Jardetzky TS, EMBO J. 2003 Apr 1;22(7):1555-66. PMID:12660162

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