2bhk: Difference between revisions

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==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 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.

==Disease==

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[[Category: preformed receptor dimer]]

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@@ Line 4: / Line 4: @@
 ==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 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.
 ==Disease==
@@ Line 31: / Line 31: @@
 [[Category: preformed receptor dimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:24:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:51 2008''