2r53

From Proteopedia

(Difference between revisions)

Revision as of 04:14, 2 July 2021

Crystal structure analysis of Bone Morphogenetic Protein-6 variant B2 (B2-BMP-6)

Structural highlights

2r53 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3bmp, 1rew, 2h62, 2h64, 2r52
Gene:	BMP6, VGR (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BMP6_HUMAN] Induces cartilage and bone formation.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Saremba S, Nickel J, Seher A, Kotzsch A, Sebald W, Mueller TD. Type I receptor binding of bone morphogenetic protein 6 is dependent on N-glycosylation of the ligand. FEBS J. 2008 Jan;275(1):172-83. Epub 2007 Dec 6. PMID:18070108 doi:10.1111/j.1742-4658.2007.06187.x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2r53"

@@ Line 1: / Line 1: @@
 ==Crystal structure analysis of Bone Morphogenetic Protein-6 variant B2 (B2-BMP-6)==
-<StructureSection load='2r53' size='340' side='right' caption='[[2r53]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='2r53' size='340' side='right'caption='[[2r53]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2r53]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R53 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2r53]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R53 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bmp|3bmp]], [[1rew|1rew]], [[2h62|2h62]], [[2h64|2h64]], [[2r52|2r52]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bmp|3bmp]], [[1rew|1rew]], [[2h62|2h62]], [[2h64|2h64]], [[2r52|2r52]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMP6, VGR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMP6, VGR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r53 OCA], [http://pdbe.org/2r53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r53 RCSB], [http://www.ebi.ac.uk/pdbsum/2r53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r53 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r53 OCA], [https://pdbe.org/2r53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r53 RCSB], [https://www.ebi.ac.uk/pdbsum/2r53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r53 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BMP6_HUMAN BMP6_HUMAN]] Induces cartilage and bone formation.
+[[https://www.uniprot.org/uniprot/BMP6_HUMAN BMP6_HUMAN]] Induces cartilage and bone formation.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r5/2r53_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r5/2r53_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 2r53" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Bone morphogenetic protein 3D structures|Bone morphogenetic protein 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Mueller, T D]]
 [[Category: Sebald, W]]

2r53

From Proteopedia

Revision as of 04:14, 2 July 2021

Crystal structure analysis of Bone Morphogenetic Protein-6 variant B2 (B2-BMP-6)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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