3bk3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_3bk3", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
OCA (talk | contribs)
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:3bk3.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_3bk3", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_3bk3|  PDB=3bk3  |  SCENE=  }}
'''Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2'''


==Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2==
<StructureSection load='3bk3' size='340' side='right'caption='[[3bk3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bk3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BK3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=3bk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bk3 OCA], [https://pdbe.org/3bk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bk3 RCSB], [https://www.ebi.ac.uk/pdbsum/3bk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bk3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BMP2_HUMAN BMP2_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/bk/3bk3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bk3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crossveinless 2 (CV-2) is an extracellular BMP modulator protein belonging to the Chordin family. During development it is expressed at sites of high BMP signaling and like Chordin CV-2 can either enhance or inhibit BMP activity. CV-2 binds to BMP-2 via its N-terminal Von Willebrand factor type C (VWC) domain 1. Here we report the structure of the complex between CV-2 VWC1 and BMP-2. The tripartite VWC1 binds BMP-2 only through a short N-terminal segment, called clip, and subdomain (SD) 1. Mutational analysis establishes that the clip segment and SD1 together create high-affinity BMP-2 binding. All four receptor-binding sites of BMP-2 are blocked in the complex, demonstrating that VWC1 acts as competitive inhibitor for all receptor types. In vivo experiments reveal that the BMP-enhancing (pro-BMP) activity of CV-2 is independent of BMP-2 binding by VWC1, showing that pro- and anti-BMP activities are structurally separated in CV-2.


==Overview==
Crystal structure analysis reveals how the Chordin family member crossveinless 2 blocks BMP-2 receptor binding.,Zhang JL, Qiu LY, Kotzsch A, Weidauer S, Patterson L, Hammerschmidt M, Sebald W, Mueller TD Dev Cell. 2008 May;14(5):739-50. PMID:18477456<ref>PMID:18477456</ref>
Crossveinless 2 (CV-2) is an extracellular BMP modulator protein belonging to the Chordin family. During development it is expressed at sites of high BMP signaling and like Chordin CV-2 can either enhance or inhibit BMP activity. CV-2 binds to BMP-2 via its N-terminal Von Willebrand factor type C (VWC) domain 1. Here we report the structure of the complex between CV-2 VWC1 and BMP-2. The tripartite VWC1 binds BMP-2 only through a short N-terminal segment, called clip, and subdomain (SD) 1. Mutational analysis establishes that the clip segment and SD1 together create high-affinity BMP-2 binding. All four receptor-binding sites of BMP-2 are blocked in the complex, demonstrating that VWC1 acts as competitive inhibitor for all receptor types. In vivo experiments reveal that the BMP-enhancing (pro-BMP) activity of CV-2 is independent of BMP-2 binding by VWC1, showing that pro- and anti-BMP activities are structurally separated in CV-2.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
3BK3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK3 OCA].
</div>
<div class="pdbe-citations 3bk3" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure analysis reveals how the Chordin family member crossveinless 2 blocks BMP-2 receptor binding., Zhang JL, Qiu LY, Kotzsch A, Weidauer S, Patterson L, Hammerschmidt M, Sebald W, Mueller TD, Dev Cell. 2008 May;14(5):739-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18477456 18477456]
*[[Bone morphogenetic protein 3D structures|Bone morphogenetic protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Danio rerio]]
[[Category: Danio rerio]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Mueller, T D.]]
[[Category: Mueller TD]]
[[Category: Sebald, W.]]
[[Category: Sebald W]]
[[Category: Zhang, J L.]]
[[Category: Zhang J-L]]
[[Category: Bmp inhibitor]]
[[Category: Bmp modulator protein]]
[[Category: Chondrogenesis]]
[[Category: Chordin]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Cytokine]]
[[Category: Developmental protein]]
[[Category: Differentiation]]
[[Category: Glycoprotein]]
[[Category: Growth factor]]
[[Category: Hormone/growth factor complex]]
[[Category: Osteogenesis]]
[[Category: Polymorphism]]
[[Category: Secreted]]
[[Category: Tgf-beta superfamily]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:19:23 2008''

Latest revision as of 05:42, 17 October 2024

Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2

3bk3, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA