1kgy

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(New page: 200px<br /><applet load="1kgy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kgy, resolution 2.7&Aring;" /> '''Crystal Structure of ...)
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caption="1kgy, resolution 2.7&Aring;" />
'''Crystal Structure of the EphB2-ephrinB2 complex'''<br />
'''Crystal Structure of the EphB2-ephrinB2 complex'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1KGY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KGY OCA].
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1KGY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGY OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Transferase]]
[[Category: Transferase]]
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[[Category: Cowan, C.A.]]
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[[Category: Cowan, C A.]]
[[Category: Henkemeyer, M.]]
[[Category: Henkemeyer, M.]]
[[Category: Himanen, J-P.]]
[[Category: Himanen, J-P.]]
[[Category: Lackmann, M.]]
[[Category: Lackmann, M.]]
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[[Category: Nikolov, D.B.]]
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[[Category: Nikolov, D B.]]
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[[Category: Rajashankar, K.R.]]
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[[Category: Rajashankar, K R.]]
[[Category: developmental protein]]
[[Category: developmental protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:12:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:06 2008''

Revision as of 11:34, 21 February 2008


1kgy, resolution 2.7Å

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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. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 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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