1rhf
From Proteopedia
(New page: 200px<br /> <applet load="1rhf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rhf, resolution 1.96Å" /> '''Crystal Structure o...) |
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| - | [[Image:1rhf.gif|left|200px]]<br /> | + | [[Image:1rhf.gif|left|200px]]<br /><applet load="1rhf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rhf" size=" | + | |
caption="1rhf, resolution 1.96Å" /> | caption="1rhf, resolution 1.96Å" /> | ||
'''Crystal Structure of human Tyro3-D1D2'''<br /> | '''Crystal Structure of human Tyro3-D1D2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The receptor Tyro3 together with Axl and Mer form the Axl/Tyro3 family of | + | The receptor Tyro3 together with Axl and Mer form the Axl/Tyro3 family of receptor tyrosine kinases. Members of this family play essential roles in spermatogenesis, immunoregulation, and phagocytosis. Gas6, the product of growth arrest-specific gene, activates the kinase activity of all three receptors. Here, we report the first biochemical and structural characterization of a member of this family, namely of a fragment spanning the two N-terminal Ig domains of the extracellular part of human Tyro3. Its ligand binding specificity profile is identical to the activation profile of the native receptor. The 1.95-A crystal structure suggests a common ligand-binding site in this receptor family located at the interface of the Ig domains and unusually rich in cis-prolines. Furthermore, both in the crystal and in solution we observed the ligand-independent dimerization of the receptor fragment. This homophilic interaction emphasizes previous functional reports, which hinted that in addition to signal transduction, members of this family of receptors might participate in cell adhesion. |
==About this Structure== | ==About this Structure== | ||
| - | 1RHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, ACT and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1RHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1RHF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dahlback, B.]] | [[Category: Dahlback, B.]] | ||
[[Category: Heiring, C.]] | [[Category: Heiring, C.]] | ||
| - | [[Category: Muller, Y | + | [[Category: Muller, Y A.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: EPE]] | [[Category: EPE]] | ||
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[[Category: mutational analysis]] | [[Category: mutational analysis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:56 2008'' |
Revision as of 12:50, 21 February 2008
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Crystal Structure of human Tyro3-D1D2
Overview
The receptor Tyro3 together with Axl and Mer form the Axl/Tyro3 family of receptor tyrosine kinases. Members of this family play essential roles in spermatogenesis, immunoregulation, and phagocytosis. Gas6, the product of growth arrest-specific gene, activates the kinase activity of all three receptors. Here, we report the first biochemical and structural characterization of a member of this family, namely of a fragment spanning the two N-terminal Ig domains of the extracellular part of human Tyro3. Its ligand binding specificity profile is identical to the activation profile of the native receptor. The 1.95-A crystal structure suggests a common ligand-binding site in this receptor family located at the interface of the Ig domains and unusually rich in cis-prolines. Furthermore, both in the crystal and in solution we observed the ligand-independent dimerization of the receptor fragment. This homophilic interaction emphasizes previous functional reports, which hinted that in addition to signal transduction, members of this family of receptors might participate in cell adhesion.
About this Structure
1RHF is a Single protein structure of sequence from Homo sapiens with , and as ligands. 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
Ligand recognition and homophilic interactions in Tyro3: structural insights into the Axl/Tyro3 receptor tyrosine kinase family., Heiring C, Dahlback B, Muller YA, J Biol Chem. 2004 Feb 20;279(8):6952-8. Epub 2003 Nov 17. PMID:14623883
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