1g5v
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SMN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SMN1 ([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=1g5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5v OCA], [http://www.ebi.ac.uk/pdbsum/1g5v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g5v RCSB]</span> | ||
}} | }} | ||
| Line 16: | Line 19: | ||
==Disease== | ==Disease== | ||
| - | Known | + | Known disease associated with this structure: Spinal muscular atrophy-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600354 600354]], Spinal muscular atrophy-2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600354 600354]], Spinal muscular atrophy-3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600354 600354]], Spinal muscular atrophy-4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600354 600354]] |
==About this Structure== | ==About this Structure== | ||
| Line 33: | Line 36: | ||
[[Category: mrna processing]] | [[Category: mrna processing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:18 2008'' |
Revision as of 17:37, 30 March 2008
| |||||||
| Gene: | SMN1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF THE HUMAN SMN PROTEIN
Contents |
Overview
Spinal muscular atrophy (SMA) is a common motor neuron disease that results from mutations in the Survival of Motor Neuron (SMN) gene. The SMN protein plays a crucial role in the assembly of spliceosomal uridine-rich small nuclear ribonucleoprotein (U snRNP) complexes via binding to the spliceosomal Sm core proteins. SMN contains a central Tudor domain that facilitates the SMN-Sm protein interaction. A SMA-causing point mutation (E134K) within the SMN Tudor domain prevents Sm binding. Here, we have determined the three-dimensional structure of the Tudor domain of human SMN. The structure exhibits a conserved negatively charged surface that is shown to interact with the C-terminal Arg and Gly-rich tails of Sm proteins. The E134K mutation does not disrupt the Tudor structure but affects the charge distribution within this binding site. An intriguing structural similarity between the Tudor domain and the Sm proteins suggests the presence of an additional binding interface that resembles that in hetero-oligomeric complexes of Sm proteins. Our data provide a structural basis for a molecular defect underlying SMA.
Disease
Known disease associated with this structure: Spinal muscular atrophy-1 OMIM:[600354], Spinal muscular atrophy-2 OMIM:[600354], Spinal muscular atrophy-3 OMIM:[600354], Spinal muscular atrophy-4 OMIM:[600354]
About this Structure
1G5V is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
SMN tudor domain structure and its interaction with the Sm proteins., Selenko P, Sprangers R, Stier G, Buhler D, Fischer U, Sattler M, Nat Struct Biol. 2001 Jan;8(1):27-31. PMID:11135666
Page seeded by OCA on Sun Mar 30 20:37:18 2008
