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| - | [[Image:2r53.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2r53| PDB=2r53 | SCENE= }} | | {{STRUCTURE_2r53| PDB=2r53 | SCENE= }} |
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| - | '''Crystal structure analysis of Bone Morphogenetic Protein-6 variant B2 (B2-BMP-6)'''
| + | ===Crystal structure analysis of Bone Morphogenetic Protein-6 variant B2 (B2-BMP-6)=== |
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| - | ==Overview==
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| - | Bone morphogenetic proteins (BMPs), together with transforming growth factor (TGF)-beta and activins/inhibins, constitute the TGF-beta superfamily of ligands. This superfamily is formed by more than 30 structurally related secreted proteins. The crystal structure of human BMP-6 was determined to a resolution of 2.1 A; the overall structure is similar to that of other TGF-beta superfamily ligands, e.g. BMP-7. The asymmetric unit contains the full dimeric BMP-6, indicating possible asymmetry between the two monomeric subunits. Indeed, the conformation of several loops differs between both monomers. In particular, the prehelix loop, which plays a crucial role in the type I receptor interactions of BMP-2, adopts two rather different conformations in BMP-6, indicating possible dynamic flexibility of the prehelix loop in its unbound conformation. Flexibility of this loop segment has been discussed as an important feature required for promiscuous binding of different type I receptors to BMPs. Further studies investigating the interaction of BMP-6 with different ectodomains of type I receptors revealed that N-glycosylation at Asn73 of BMP-6 in the wrist epitope is crucial for recognition by the activin receptor type I. In the absence of the carbohydrate moiety, activin receptor type I-mediated signaling of BMP-6 is totally diminished. Thus, flexibility within the binding epitope of BMP-6 and an unusual recognition motif, i.e. an N-glycosylation motif, possibly play an important role in type I receptor specificity of BMP-6.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18070108}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18070108 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18070108}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tgf-beta ligand]] | | [[Category: Tgf-beta ligand]] |
| | [[Category: Vgr]] | | [[Category: Vgr]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:15:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:04:34 2008'' |
Revision as of 01:04, 28 July 2008
Template:STRUCTURE 2r53
Crystal structure analysis of Bone Morphogenetic Protein-6 variant B2 (B2-BMP-6)
Template:ABSTRACT PUBMED 18070108
About this Structure
2R53 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Type I receptor binding of bone morphogenetic protein 6 is dependent on N-glycosylation of the ligand., Saremba S, Nickel J, Seher A, Kotzsch A, Sebald W, Mueller TD, FEBS J. 2008 Jan;275(1):172-83. Epub 2007 Dec 6. PMID:18070108
Page seeded by OCA on Mon Jul 28 04:04:34 2008
