1kgy
From Proteopedia
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- | [[Image:1kgy.gif|left|200px]] | + | [[Image:1kgy.gif|left|200px]] |
- | + | ||
- | '''Crystal Structure of the EphB2-ephrinB2 complex''' | + | {{Structure |
+ | |PDB= 1kgy |SIZE=350|CAPTION= <scene name='initialview01'>1kgy</scene>, resolution 2.7Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of the EphB2-ephrinB2 complex''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1KGY is a [ | + | 1KGY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGY OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of an Eph receptor-ephrin complex., Himanen JP, Rajashankar KR, Lackmann M, Cowan CA, Henkemeyer M, Nikolov DB, Nature. 2001 Dec 20-27;414(6866):933-8. PMID:[http:// | + | Crystal structure of an Eph receptor-ephrin complex., Himanen JP, Rajashankar KR, Lackmann M, Cowan CA, Henkemeyer M, Nikolov DB, Nature. 2001 Dec 20-27;414(6866):933-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11780069 11780069] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: developmental protein]] | [[Category: developmental protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:17:19 2008'' |
Revision as of 10:17, 20 March 2008
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, resolution 2.7Å | |||||||
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Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of the EphB2-ephrinB2 complex
Overview
The Eph family of receptor tyrosine kinases and their membrane-anchored ephrin ligands are important in regulating cell-cell interactions as they initiate a unique bidirectional signal transduction cascade whereby information is communicated into both the Eph-expressing and the ephrin-expressing cells. Initially identified as regulators of axon pathfinding and neuronal cell migration, Ephs and ephrins are now known to have roles in many other cell-cell interactions, including those of vascular endothelial cells and specialized epithelia. Here we report the crystal structure of the complex formed between EphB2 and ephrin-B2, determined at 2.7 A resolution. Each Eph receptor binds an ephrin ligand through an expansive dimerization interface dominated by the insertion of an extended ephrin loop into a channel at the surface of the receptor. Two Eph-Ephrin dimers then join to form a tetramer, in which each ligand interacts with two receptors and each receptor interacts with two ligands. The Eph and ephrin molecules are precisely positioned and orientated in these complexes, promoting higher-order clustering and the initiation of bidirectional signalling.
About this Structure
1KGY is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of an Eph receptor-ephrin complex., Himanen JP, Rajashankar KR, Lackmann M, Cowan CA, Henkemeyer M, Nikolov DB, Nature. 2001 Dec 20-27;414(6866):933-8. PMID:11780069
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