1ich
From Proteopedia
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| - | [[Image:1ich.gif|left|200px]] | + | [[Image:1ich.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR RECEPTOR-1 DEATH DOMAIN''' | + | {{Structure |
| + | |PDB= 1ich |SIZE=350|CAPTION= <scene name='initialview01'>1ich</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR RECEPTOR-1 DEATH DOMAIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ICH is a [ | + | 1ICH is a [[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=1ICH OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of the tumor necrosis factor receptor-1 death domain., Sukits SF, Lin LL, Hsu S, Malakian K, Powers R, Xu GY, J Mol Biol. 2001 Jul 20;310(4):895-906. PMID:[http:// | + | Solution structure of the tumor necrosis factor receptor-1 death domain., Sukits SF, Lin LL, Hsu S, Malakian K, Powers R, Xu GY, J Mol Biol. 2001 Jul 20;310(4):895-906. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11453696 11453696] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: death domain]] | [[Category: death domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:29 2008'' |
Revision as of 09:48, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR RECEPTOR-1 DEATH DOMAIN
Contents |
Overview
Tumor necrosis factor receptor-1 death domain (TNFR-1 DD) is the intracellular functional domain responsible for the receptor signaling activities. The solution structure of the R347K mutant of TNFR-1 DD was solved by NMR spectroscopy. A total of 20 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 1167 distance constraints and 117 torsion angle constraints. The atomic rms distribution about the mean coordinate positions for the 20 structures for residues composing the secondary structure region is 0.40 A for the backbone atoms and 1.09 A for all atoms. The structure consists of six antiparallel alpha-helices arranged in a similar fashion to the other members of the death domain superfamily. The secondary structure and three-dimensional structure of R347K TNFR1-DD are very similar to the secondary structure and deduced topology of the R347A TNFR1-DD mutant. Mutagenesis studies identified critical residues located in alpha2 and part of alpha3 and alpha4 that are crucial for self-interaction and interaction with TRADD. Structural superposition with previously solved proteins in the death domain superfamily reveals that the major differences between the structures reside in alpha2, alpha3, and alpha4. Interestingly, these regions correspond to the binding sites of TNFR1-DD, providing a structural basis for the specificity of death domain interactions and its subsequent signaling event.
Disease
Known diseases associated with this structure: Periodic fever, familial OMIM:[191190]
About this Structure
1ICH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the tumor necrosis factor receptor-1 death domain., Sukits SF, Lin LL, Hsu S, Malakian K, Powers R, Xu GY, J Mol Biol. 2001 Jul 20;310(4):895-906. PMID:11453696
Page seeded by OCA on Thu Mar 20 11:48:29 2008
