1nuk

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[[Image:1nuk.gif|left|200px]]<br /><applet load="1nuk" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nuk.gif|left|200px]]
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caption="1nuk, resolution 2.9&Aring;" />
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'''CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE'''<br />
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{{Structure
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|PDB= 1nuk |SIZE=350|CAPTION= <scene name='initialview01'>1nuk</scene>, resolution 2.9&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NUK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1NUK OCA].
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1NUK is a [[Single protein]] structure of sequence 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=1NUK OCA].
==Reference==
==Reference==
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Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2., Himanen JP, Henkemeyer M, Nikolov DB, Nature. 1998 Dec 3;396(6710):486-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9853759 9853759]
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Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2., Himanen JP, Henkemeyer M, Nikolov DB, Nature. 1998 Dec 3;396(6710):486-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9853759 9853759]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:57 2008''

Revision as of 11:02, 20 March 2008


PDB ID 1nuk

Drag the structure with the mouse to rotate
, resolution 2.9Å
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 LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE


Overview

The Eph receptors, which bind a group of cell-membrane-anchored ligands known as ephrins, represent the largest subfamily of receptor tyrosine kinases (RTKs). They are predominantly expressed in the developing and adult nervous system and are important in contact-mediated axon guidance, axon fasciculation and cell migration. Eph receptors are unique among other RTKs in that they fall into two subclasses with distinct ligand specificities, and in that they can themselves function as ligands to activate bidirectional cell-cell signalling. We report here the crystal structure at 2.9 A resolution of the amino-terminal ligand-binding domain of the EphB2 receptor (also known as Nuk). The domain folds into a compact jellyroll beta-sandwich composed of 11 antiparallel beta-strands. Using structure-based mutagenesis, we have identified an extended loop that is important for ligand binding and class specificity. This loop, which is conserved within but not between Eph RTK subclasses, packs against the concave beta-sandwich surface near positions at which missense mutations cause signalling defects, localizing the ligand-binding region on the surface of the receptor.

About this Structure

1NUK is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2., Himanen JP, Henkemeyer M, Nikolov DB, Nature. 1998 Dec 3;396(6710):486-91. PMID:9853759

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