2gy7: Difference between revisions

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New page: left|200px<br /> <applet load="2gy7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gy7, resolution 3.700Å" /> '''Angiopoietin-2/Tie...
 
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[[Image:2gy7.gif|left|200px]]<br />
[[Image:2gy7.gif|left|200px]]<br /><applet load="2gy7" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2gy7" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2gy7, resolution 3.700&Aring;" />
caption="2gy7, resolution 3.700&Aring;" />
'''Angiopoietin-2/Tie2 Complex Crystal Structure'''<br />
'''Angiopoietin-2/Tie2 Complex Crystal Structure'''<br />


==Overview==
==Overview==
The Tie receptor tyrosine kinases and their angiopoietin (Ang) ligands, play central roles in developmental and tumor-induced angiogenesis. Here, we present the crystal structures of the Tie2 ligand-binding region alone, and in complex with Ang2. In contrast to prediction, Tie2 contains not two, but three immunoglobulin (Ig) domains, which fold together with the three, epidermal growth factor domains into a compact, arrowhead-shaped, structure. Ang2 binds at the tip of the arrowhead utilizing a lock-and-key, mode of ligand recognition-unique for a receptor kinase-where two, complementary surfaces interact with each other with no domain, rearrangements and little conformational change in either molecule., Ang2-Tie2 recognition is similar to antibody-protein antigen recognition, including the location of the ligand-binding site within the Ig fold., Analysis of the structures and structure-based mutagenesis provide insight, into the mechanism of receptor activation and support the hypothesis that, all angiopoietins interact with Tie2 in a structurally similar manner.
The Tie receptor tyrosine kinases and their angiopoietin (Ang) ligands play central roles in developmental and tumor-induced angiogenesis. Here we present the crystal structures of the Tie2 ligand-binding region alone and in complex with Ang2. In contrast to prediction, Tie2 contains not two but three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. Ang2 binds at the tip of the arrowhead utilizing a lock-and-key mode of ligand recognition-unique for a receptor kinase-where two complementary surfaces interact with each other with no domain rearrangements and little conformational change in either molecule. Ang2-Tie2 recognition is similar to antibody-protein antigen recognition, including the location of the ligand-binding site within the Ig fold. Analysis of the structures and structure-based mutagenesis provide insight into the mechanism of receptor activation and support the hypothesis that all angiopoietins interact with Tie2 in a structurally similar manner.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2GY7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GY7 OCA].  
2GY7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GY7 OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Receptor protein-tyrosine kinase]]
[[Category: Receptor protein-tyrosine kinase]]
[[Category: Barton, W.A.]]
[[Category: Barton, W A.]]
[[Category: Nikolov, D.B.]]
[[Category: Nikolov, D B.]]
[[Category: CA]]
[[Category: CA]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: receptor-ligand complex]]
[[Category: receptor-ligand complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:23:44 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:20 2008''

Revision as of 18:36, 21 February 2008

File:2gy7.gif


2gy7, resolution 3.700Å

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Angiopoietin-2/Tie2 Complex Crystal Structure

OverviewOverview

The Tie receptor tyrosine kinases and their angiopoietin (Ang) ligands play central roles in developmental and tumor-induced angiogenesis. Here we present the crystal structures of the Tie2 ligand-binding region alone and in complex with Ang2. In contrast to prediction, Tie2 contains not two but three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. Ang2 binds at the tip of the arrowhead utilizing a lock-and-key mode of ligand recognition-unique for a receptor kinase-where two complementary surfaces interact with each other with no domain rearrangements and little conformational change in either molecule. Ang2-Tie2 recognition is similar to antibody-protein antigen recognition, including the location of the ligand-binding site within the Ig fold. Analysis of the structures and structure-based mutagenesis provide insight into the mechanism of receptor activation and support the hypothesis that all angiopoietins interact with Tie2 in a structurally similar manner.

DiseaseDisease

Known diseases associated with this structure: Venous malformations, multiple cutaneous and mucosal OMIM:[600221]

About this StructureAbout this Structure

2GY7 is a Protein complex structure of sequences from Homo sapiens with , and as ligands. Active as Receptor protein-tyrosine kinase, with EC number 2.7.10.1 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex., Barton WA, Tzvetkova-Robev D, Miranda EP, Kolev MV, Rajashankar KR, Himanen JP, Nikolov DB, Nat Struct Mol Biol. 2006 Jun;13(6):524-32. Epub 2006 May 28. PMID:16732286

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