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.


1g82

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1g82.gif|left|200px]]<br /><applet load="1g82" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1g82.gif|left|200px]]
-
caption="1g82, resolution 2.6&Aring;" />
+
 
-
'''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9'''<br />
+
{{Structure
 +
|PDB= 1g82 |SIZE=350|CAPTION= <scene name='initialview01'>1g82</scene>, resolution 2.6&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1G82 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G82 OCA].
+
1G82 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G82 OCA].
==Reference==
==Reference==
-
Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces., Hecht HJ, Adar R, Hofmann B, Bogin O, Weich H, Yayon A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):378-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11223514 11223514]
+
Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces., Hecht HJ, Adar R, Hofmann B, Bogin O, Weich H, Yayon A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):378-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11223514 11223514]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 23: Line 32:
[[Category: fibroblast growth factor]]
[[Category: fibroblast growth factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:13 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:19:29 2008''

Revision as of 09:19, 20 March 2008

Image:1g82.gif


PDB ID 1g82

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF FIBROBLAST GROWTH FACTOR 9


Overview

Fibroblast growth factors (FGFs) constitute a family of at least 20 structurally related heparin-binding polypeptides active in regulating cell growth, survival, differentiation and migration. FGF9, originally discovered as a glia-activating factor, shares 30% sequence identity with other FGFs and has a unique spectrum of target-cell specificity. FGF9 crystallized in the tetragonal space group I4(1), with unit-cell parameters a = b = 151.9, c = 117.2 A. The structure of the glycosylated protein has been refined to an R value of 21.0% with R(free) = 24.8%) at 2.6 A resolution. The four molecules in the asymmetric unit are arranged in two non-crystallographic dimers, with the dimer interface composed partly of residues from N- and C-terminal extensions from the FGF core structure. Most of the receptor-binding residues identified in FGF1- and FGF2-receptor complexes are buried in the dimer interface, with the beta8-beta9 loop stabilized in a particular conformation by an intramolecular hydrogen-bonding network. The potential heparin-binding sites are in a pattern distinct from FGF1 and FGF2. The carbohydrate moiety attached at Asn79 has no structural influence.

About this Structure

1G82 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces., Hecht HJ, Adar R, Hofmann B, Bogin O, Weich H, Yayon A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):378-84. PMID:11223514

Page seeded by OCA on Thu Mar 20 11:19:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g82"
Personal tools