3bk3: Difference between revisions

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[[Image:3bk3.~~jpg~~|left|200px]]

[[Image:3bk3.png|left|200px]]

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~~'''~~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===

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_18477456}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18477456 is the PubMed ID number.

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==About this Structure==

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[[Category: Secreted]]

[[Category: Tgf-beta superfamily]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed May 28 09~~:19:23 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:23:40 2008''

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-[[Image:3bk3.jpg|left|200px]]
+{{Seed}}
+[[Image:3bk3.png|left|200px]]
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 {{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===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18477456}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18477456 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18477456}}
 ==About this Structure==
@@ Line 41: / Line 45: @@
 [[Category: Secreted]]
 [[Category: Tgf-beta superfamily]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:19:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:23:40 2008''