1yyh
From Proteopedia
(New page: 200px<br /> <applet load="1yyh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yyh, resolution 1.901Å" /> '''Crystal structure ...) |
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| - | [[Image:1yyh.gif|left|200px]]<br /> | + | [[Image:1yyh.gif|left|200px]]<br /><applet load="1yyh" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yyh" size=" | + | |
caption="1yyh, resolution 1.901Å" /> | caption="1yyh, resolution 1.901Å" /> | ||
'''Crystal structure of the human Notch 1 ankyrin domain'''<br /> | '''Crystal structure of the human Notch 1 ankyrin domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Notch receptor is part of a highly conserved signalling system of | + | The Notch receptor is part of a highly conserved signalling system of central importance to animal development. Its ANK (ankyrin) domain is required for Notch-mediated signal transduction. The crystal structure of the human Notch 1 ANK domain was solved by molecular replacement at 1.9 A (1 A=0.1 nm) resolution, and it shows that the features identified in the Drosophila homologue are conserved. The domain has six of the seven ANK repeats predicted from sequence. The putative first repeat, which has only part of the consensus and a long insertion, is disordered in both molecules in the asymmetric unit, possibly due to the absence of the RAM (RBPJkappa-associated molecule) region N-terminal to it. The exposed hydrophobic core is involved in intermolecular interactions in the crystal. Evolutionary trace analysis identified several residues that map to the hairpins of the structure and may be of functional importance. Based on the Notch 1 ANK structure and analysis of homologous Notch ANK sequences, we predict two possible binding sites on the domain: one on the concave surface of repeat 2 and the other below the hairpins of repeats 6-7. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1YYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blundell, T | + | [[Category: Blundell, T L.]] |
| - | [[Category: Chirgadze, D | + | [[Category: Chirgadze, D Y.]] |
| - | [[Category: Ehebauer, M | + | [[Category: Ehebauer, M T.]] |
[[Category: Hayward, P.]] | [[Category: Hayward, P.]] | ||
[[Category: Martinez-Arias, A.]] | [[Category: Martinez-Arias, A.]] | ||
[[Category: ankyrin repeats; notch 1]] | [[Category: ankyrin repeats; notch 1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:22 2008'' |
Revision as of 14:10, 21 February 2008
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Crystal structure of the human Notch 1 ankyrin domain
Contents |
Overview
The Notch receptor is part of a highly conserved signalling system of central importance to animal development. Its ANK (ankyrin) domain is required for Notch-mediated signal transduction. The crystal structure of the human Notch 1 ANK domain was solved by molecular replacement at 1.9 A (1 A=0.1 nm) resolution, and it shows that the features identified in the Drosophila homologue are conserved. The domain has six of the seven ANK repeats predicted from sequence. The putative first repeat, which has only part of the consensus and a long insertion, is disordered in both molecules in the asymmetric unit, possibly due to the absence of the RAM (RBPJkappa-associated molecule) region N-terminal to it. The exposed hydrophobic core is involved in intermolecular interactions in the crystal. Evolutionary trace analysis identified several residues that map to the hairpins of the structure and may be of functional importance. Based on the Notch 1 ANK structure and analysis of homologous Notch ANK sequences, we predict two possible binding sites on the domain: one on the concave surface of repeat 2 and the other below the hairpins of repeats 6-7.
Disease
Known diseases associated with this structure: Aortic valve disease OMIM:[190198], Leukemia, T-cell acute lymphoblastic OMIM:[190198]
About this Structure
1YYH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structure of the human Notch 1 ankyrin domain., Ehebauer MT, Chirgadze DY, Hayward P, Martinez Arias A, Blundell TL, Biochem J. 2005 Nov 15;392(Pt 1):13-20. PMID:16011479
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