1lr8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lr8.gif|left|200px]]<br /><applet load="1lr8" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1lr8.gif|left|200px]]
-
caption="1lr8, resolution 2.10&Aring;" />
+
 
-
'''Crystal structure of Fs1, the heparin-binding domain of follistatin, complexed with the heparin analogue D-myo-inositol hexasulphate (Ins6S)'''<br />
+
{{Structure
 +
|PDB= 1lr8 |SIZE=350|CAPTION= <scene name='initialview01'>1lr8</scene>, resolution 2.10&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=IHS:D-MYO-INOSITOL-HEXASULPHATE'>IHS</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of Fs1, the heparin-binding domain of follistatin, complexed with the heparin analogue D-myo-inositol hexasulphate (Ins6S)'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1LR8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=IHS:'>IHS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR8 OCA].
+
1LR8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR8 OCA].
==Reference==
==Reference==
-
Crystal structures of the heparan sulfate-binding domain of follistatin. Insights into ligand binding., Innis CA, Hyvonen M, J Biol Chem. 2003 Oct 10;278(41):39969-77. Epub 2003 Jul 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12867435 12867435]
+
Crystal structures of the heparan sulfate-binding domain of follistatin. Insights into ligand binding., Innis CA, Hyvonen M, J Biol Chem. 2003 Oct 10;278(41):39969-77. Epub 2003 Jul 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12867435 12867435]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 19: Line 28:
[[Category: d-myo-inositol hexasulphate]]
[[Category: d-myo-inositol hexasulphate]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:37 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:34:13 2008''

Revision as of 10:34, 20 March 2008


PDB ID 1lr8

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Fs1, the heparin-binding domain of follistatin, complexed with the heparin analogue D-myo-inositol hexasulphate (Ins6S)


Overview

Follistatin associates with transforming growth factor-beta-like growth factors such as activin or bone morphogenetic proteins to form an inactive complex, thereby regulating processes as diverse as embryonic development and cell secretion. Although an interaction between heparan sulfate chains present at the cell surface and follistatin has been recorded, the impact of this binding reaction on the follistatin-mediated inhibition of transforming growth factor-beta-like signaling remains unclear. To gain a structural insight into this interaction, we have solved the crystal structure of the presumed heparan sulfate-binding domain of follistatin, both alone and in complex with the small heparin analogs sucrose octasulfate and D-myo-inositol hexasulfate. In addition, we have confirmed the binding of the sucrose octasulfate and D-myo-inositol hexasulfate molecules to this follistatin domain and determined the association constants and stoichiometries of both interactions in solution using isothermal titration calorimetry. Overall, our results shed light upon the structure of this follistatin domain and reveal a novel conformation for a hinge region connecting epidermal growth factor-like and Kazal-like subdomains compared with the follistatin-like domain found in the extracellular matrix protein BM-40. Moreover, the crystallographic analysis of the two protein-ligand complexes mentioned above leads us to propose a potential location for the heparan sulfate-binding site on the surface of follistatin and to suggest the involvement of residues Asn80 and Arg86 in such a follistatin-heparin interaction.

About this Structure

1LR8 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structures of the heparan sulfate-binding domain of follistatin. Insights into ligand binding., Innis CA, Hyvonen M, J Biol Chem. 2003 Oct 10;278(41):39969-77. Epub 2003 Jul 16. PMID:12867435

Page seeded by OCA on Thu Mar 20 12:34:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools