We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2hlr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hlr.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2hlr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hlr| PDB=2hlr | SCENE= }}
{{STRUCTURE_2hlr| PDB=2hlr | SCENE= }}
-
'''Crystal Structure of the Extracellular Domain of the Type II BMP Receptor'''
+
===Crystal Structure of the Extracellular Domain of the Type II BMP Receptor===
-
==Overview==
+
<!--
-
BMPRII is a type II TGF-beta serine threonine kinase receptor which is integral to the bone morphogenetic protein (BMP) signalling pathway. It is known to bind BMP and growth differentiation factor (GDF) ligands, and has overlapping ligand specificity with the activin type II receptor, ActRII. In contrast to activin and TGF-beta type ligands, BMPs bind to type II receptors with lower affinity than type I receptors. Crystals of the BMPRII ectodomain were grown in two different forms, both of which diffracted to high resolution. The tetragonal form exhibited some disorder, whereas the entire polypeptide was seen in the orthorhombic form. The two structures retain the basic three-finger toxin fold of other TGF-beta receptor ectodomains, and share the main hydrophobic patch used by ActRII to bind various ligands. However, they present different conformations of the A-loop at the periphery of the proposed ligand-binding interface, in conjunction with rearrangement of a disulfide bridge within the loop. This particular disulfide (Cys94-Cys117) is only present in BMPRII and activin receptors, suggesting that it is important for their likely shared mode of binding. Evidence is presented that the two crystal forms represent ligand-bound and free conformations of BMPRII. Comparison with the solved structure of ActRII bound to BMP2 suggests that His87, unique amongst TGF-beta receptors, may play a key role in ligand recognition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17094948}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17094948 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17094948}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Tgf-beta]]
[[Category: Tgf-beta]]
[[Category: Three-finger toxin]]
[[Category: Three-finger toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:26:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:28:52 2008''

Revision as of 15:28, 27 July 2008

Image:2hlr.png

Template:STRUCTURE 2hlr

Crystal Structure of the Extracellular Domain of the Type II BMP Receptor

Template:ABSTRACT PUBMED 17094948

About this Structure

2HLR is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.

Reference

High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: implications for ligand binding., Mace PD, Cutfield JF, Cutfield SM, Biochem Biophys Res Commun. 2006 Dec 29;351(4):831-8. Epub 2006 Nov 10. PMID:17094948

Page seeded by OCA on Sun Jul 27 18:28:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hlr"
Personal tools