1yyh
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= NOTCH1, TAN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= NOTCH1, TAN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yyh OCA], [http://www.ebi.ac.uk/pdbsum/1yyh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yyh RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Aortic valve disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190198 190198]], Leukemia, T-cell acute lymphoblastic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190198 190198]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Hayward, P.]] | [[Category: Hayward, P.]] | ||
[[Category: Martinez-Arias, A.]] | [[Category: Martinez-Arias, A.]] | ||
| - | [[Category: ankyrin | + | [[Category: ankyrin repeat]] |
| + | [[Category: notch 1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:26:23 2008'' |
Revision as of 22:26, 30 March 2008
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| , resolution 1.901Å | |||||||
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| Gene: | NOTCH1, TAN1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the human Notch 1 ankyrin domain
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.
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
Page seeded by OCA on Mon Mar 31 01:26:23 2008
