2hlr

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[[Image:2hlr.gif|left|200px]]<br /><applet load="2hlr" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hlr.gif|left|200px]]
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caption="2hlr, resolution 1.200&Aring;" />
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'''Crystal Structure of the Extracellular Domain of the Type II BMP Receptor'''<br />
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{{Structure
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|PDB= 2hlr |SIZE=350|CAPTION= <scene name='initialview01'>2hlr</scene>, resolution 1.200&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Receptor_protein_serine/threonine_kinase Receptor protein serine/threonine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.30 2.7.11.30]
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|GENE= BMPRII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9940 Ovis aries])
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}}
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'''Crystal Structure of the Extracellular Domain of the Type II BMP Receptor'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2HLR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Active as [http://en.wikipedia.org/wiki/Receptor_protein_serine/threonine_kinase Receptor protein serine/threonine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.30 2.7.11.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLR OCA].
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2HLR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLR OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17094948 17094948]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17094948 17094948]
[[Category: Ovis aries]]
[[Category: Ovis aries]]
[[Category: Receptor protein serine/threonine kinase]]
[[Category: Receptor protein serine/threonine kinase]]
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[[Category: three-finger toxin]]
[[Category: three-finger toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:18:36 2008''

Revision as of 15:18, 20 March 2008


PDB ID 2hlr

Drag the structure with the mouse to rotate
, resolution 1.200Å
Gene: BMPRII (Ovis aries)
Activity: Receptor protein serine/threonine kinase, with EC number 2.7.11.30
Coordinates: save as pdb, mmCIF, xml



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.

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

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