2bhk: Difference between revisions

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[[Image:2bhk.~~gif~~|left|200px]]

[[Image:2bhk.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF HUMAN GROWTH AND DIFFERENTIATION FACTOR 5 (GDF5)~~'''~~

===CRYSTAL STRUCTURE OF HUMAN GROWTH AND DIFFERENTIATION FACTOR 5 (GDF5)===

~~==Overview==~~

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The ~~crystal structure of human growth differentiation factor 5~~ (~~GDF5) was solved~~ at 2.~~4A resolution~~. ~~The structure is very similar to the structure of bone morphogenetic factor 7 (BMP7~~) ~~and consists of two banana-shaped monomers~~, ~~linked via a disulfide bridge. The crystal packing of GDF5~~ is the ~~same as the crystal packing of BMP7~~. ~~This is highly unusual since only 25~~-~~30% of the crystal contacts involve identical residues. Analysis of the crystal packing revealed that residues of the type I receptor epitope are binding to residues of the type II receptor~~-binding epitope. The fact that for both BMP family members the type I and type II receptor-binding sites interact suggests that the complementary sites on the receptors may interact as well, suggesting a way how preformed receptor heterodimers may form, similar to the preformed receptors observed for the erythropoietin receptor and the BMP2 receptors.

The line below this paragraph, {{ABSTRACT_PUBMED_15752764}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15752764 is the PubMed ID number.

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==About this Structure==

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[[Category: Hormone-receptor interaction]]

[[Category: Preformed receptor dimer]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 20~~:17:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:57:26 2008''

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-[[Image:2bhk.gif|left|200px]]
+{{Seed}}
+[[Image:2bhk.png|left|200px]]
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 {{STRUCTURE_2bhk|  PDB=2bhk  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF HUMAN GROWTH AND DIFFERENTIATION FACTOR 5 (GDF5)'''
+===CRYSTAL STRUCTURE OF HUMAN GROWTH AND DIFFERENTIATION FACTOR 5 (GDF5)===
-==Overview==
+<!--
-The crystal structure of human growth differentiation factor 5 (GDF5) was solved at 2.4A resolution. The structure is very similar to the structure of bone morphogenetic factor 7 (BMP7) and consists of two banana-shaped monomers, linked via a disulfide bridge. The crystal packing of GDF5 is the same as the crystal packing of BMP7. This is highly unusual since only 25-30% of the crystal contacts involve identical residues. Analysis of the crystal packing revealed that residues of the type I receptor epitope are binding to residues of the type II receptor-binding epitope. The fact that for both BMP family members the type I and type II receptor-binding sites interact suggests that the complementary sites on the receptors may interact as well, suggesting a way how preformed receptor heterodimers may form, similar to the preformed receptors observed for the erythropoietin receptor and the BMP2 receptors.
+The line below this paragraph, {{ABSTRACT_PUBMED_15752764}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15752764 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15752764}}
 ==About this Structure==
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 [[Category: Hormone-receptor interaction]]
 [[Category: Preformed receptor dimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:17:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:57:26 2008''