2bhk: Difference between revisions
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|PDB= 2bhk |SIZE=350|CAPTION= <scene name='initialview01'>2bhk</scene>, resolution 2.4Å | |PDB= 2bhk |SIZE=350|CAPTION= <scene name='initialview01'>2bhk</scene>, resolution 2.4Å | ||
|SITE= <scene name='pdbsite=AC1:Ipa+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ipa+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhk OCA], [http://www.ebi.ac.uk/pdbsum/2bhk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bhk RCSB]</span> | |||
}} | }} | ||
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==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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Pohl, J.]] | [[Category: Pohl, J.]] | ||
[[Category: Schreuder, H.]] | [[Category: Schreuder, H.]] | ||
[[Category: bone morphogenetic factor]] | [[Category: bone morphogenetic factor]] | ||
[[Category: cystine knot]] | [[Category: cystine knot]] | ||
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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 Mon Mar 31 02:06:33 2008'' | ||
Revision as of 23:06, 30 March 2008
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| 2bhk, resolution 2.4Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | IPA | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
About this Structure
2BHK is a Single protein structure of sequence from Homo sapiens. 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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