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.
2bhk
From Proteopedia
| Line 6: | Line 6: | ||
==Overview== | ==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== | ||
| + | Known diseases associated with this structure: Acromesomelic dysplasia, Hunter-Thompson type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601146 601146]], Brachydactyly, type A2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601146 601146]], Brachydactyly, type C OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601146 601146]], Chondrodysplasia, Grebe type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601146 601146]], Fibular hypoplasia and complex brachydactyly OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601146 601146]], Multiple synostoses syndrome type 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601146 601146]], Symphalangism, proximal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601146 601146]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 29: | Line 32: | ||
[[Category: preformed receptor dimer]] | [[Category: preformed receptor dimer]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:02:44 2007'' |
Revision as of 18:56, 12 November 2007
|
CRYSTAL STRUCTURE OF HUMAN GROWTH AND DIFFERENTIATION FACTOR 5 (GDF5)
Contents |
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.
Disease
Known diseases associated with this structure: Acromesomelic dysplasia, Hunter-Thompson type OMIM:[601146], Brachydactyly, type A2 OMIM:[601146], Brachydactyly, type C OMIM:[601146], Chondrodysplasia, Grebe type OMIM:[601146], Fibular hypoplasia and complex brachydactyly OMIM:[601146], Multiple synostoses syndrome type 1 OMIM:[601146], Symphalangism, proximal OMIM:[601146]
About this Structure
2BHK is a Single protein structure of sequence from Homo sapiens with IPA as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structure of recombinant human growth and differentiation factor 5: evidence for interaction of the type I and type II receptor-binding sites., Schreuder H, Liesum A, Pohl J, Kruse M, Koyama M, Biochem Biophys Res Commun. 2005 Apr 15;329(3):1076-86. PMID:15752764
Page seeded by OCA on Mon Nov 12 21:02:44 2007
