1es7: Difference between revisions

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[[Image:1es7.~~gif~~|left|200px]]

[[Image:1es7.png|left|200px]]

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~~'''~~COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS~~'''~~

===COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS===

~~==Overview==~~

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~~Bone morphogenetic proteins (BMPs) belong~~ to the ~~large transforming growth factor-beta~~ (~~TGF-beta) superfamily of multifunctional cytokines~~. ~~BMP-2 can induce ectopic bone and cartilage formation in adult vertebrates and is involved in central steps in early embryonal development in animals~~. Signaling by these cytokines requires binding of two types of transmembrane serine/threonine receptor kinase chains classified as type I and type II. Here we report the crystal structure of human dimeric BMP-2 in complex with two high affinity BMP receptor IA extracellular domains (BRIAec)~~. The receptor chains bind to~~ the ~~'wrist' epitopes of the BMP-2 dimer and contact both BMP-2 monomers~~. ~~No contacts exist between the receptor domains. The model reveals the structural basis for discrimination between type I and type II receptors and the variability of receptor~~-~~ligand interactions that is seen in BMP~~-~~TGF-beta systems.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10881198}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10881198 is the PubMed ID number.

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==About this Structure==

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[[Category: Tgf beta superfamily]]

[[Category: Three finger toxin fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:27:35 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:47:49 2008''

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-[[Image:1es7.gif|left|200px]]
+{{Seed}}
+[[Image:1es7.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1es7|  PDB=1es7  |  SCENE=  }}
-'''COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS'''
+===COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS===
-==Overview==
+<!--
-Bone morphogenetic proteins (BMPs) belong to the large transforming growth factor-beta (TGF-beta) superfamily of multifunctional cytokines. BMP-2 can induce ectopic bone and cartilage formation in adult vertebrates and is involved in central steps in early embryonal development in animals. Signaling by these cytokines requires binding of two types of transmembrane serine/threonine receptor kinase chains classified as type I and type II. Here we report the crystal structure of human dimeric BMP-2 in complex with two high affinity BMP receptor IA extracellular domains (BRIAec). The receptor chains bind to the 'wrist' epitopes of the BMP-2 dimer and contact both BMP-2 monomers. No contacts exist between the receptor domains. The model reveals the structural basis for discrimination between type I and type II receptors and the variability of receptor-ligand interactions that is seen in BMP-TGF-beta systems.
+The line below this paragraph, {{ABSTRACT_PUBMED_10881198}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10881198 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10881198}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Tgf beta superfamily]]
 [[Category: Three finger toxin fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:27:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 01:47:49 2008''