2bhk: Difference between revisions
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==Overview== | ==Overview== | ||
The crystal structure of human growth differentiation factor 5 (GDF5) was | 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== | ==Disease== | ||
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[[Category: preformed receptor dimer]] | [[Category: preformed receptor dimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:51 2008'' | ||
Revision as of 14:37, 21 February 2008
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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.
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. Known structural/functional 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
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