2bhk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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 5 17:38:56 2007''
+
''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


2bhk, resolution 2.4Å

Drag the structure with the mouse to rotate

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools