2bkd
From Proteopedia
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|PDB= 2bkd |SIZE=350|CAPTION= <scene name='initialview01'>2bkd</scene> | |PDB= 2bkd |SIZE=350|CAPTION= <scene name='initialview01'>2bkd</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=HSO:HISTIDINOL'>HSO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bkd OCA], [http://www.ebi.ac.uk/pdbsum/2bkd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bkd RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
FMRP, whose lack of expression causes the X-linked fragile X syndrome, is a modular RNA binding protein thought to be involved in posttranslational regulation. We have solved the structure in solution of the N-terminal domain of FMRP (NDF), a functionally important region involved in multiple interactions. The structure consists of a composite fold comprising two repeats of a Tudor motif followed by a short alpha helix. The interactions between the three structural elements are essential for the stability of the NDF fold. Although structurally similar, the two repeats have different dynamic and functional properties. The second, more flexible repeat is responsible for interacting both with methylated lysine and with 82-FIP, one of the FMRP nuclear partners. NDF contains a 3D nucleolar localization signal, since destabilization of its fold leads to altered nucleolar localization of FMRP. We suggest that the NDF composite fold determines an allosteric mechanism that regulates the FMRP functions. | FMRP, whose lack of expression causes the X-linked fragile X syndrome, is a modular RNA binding protein thought to be involved in posttranslational regulation. We have solved the structure in solution of the N-terminal domain of FMRP (NDF), a functionally important region involved in multiple interactions. The structure consists of a composite fold comprising two repeats of a Tudor motif followed by a short alpha helix. The interactions between the three structural elements are essential for the stability of the NDF fold. Although structurally similar, the two repeats have different dynamic and functional properties. The second, more flexible repeat is responsible for interacting both with methylated lysine and with 82-FIP, one of the FMRP nuclear partners. NDF contains a 3D nucleolar localization signal, since destabilization of its fold leads to altered nucleolar localization of FMRP. We suggest that the NDF composite fold determines an allosteric mechanism that regulates the FMRP functions. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Fragile X syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=309550 309550]], Fragile X tremor/ataxia syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=309550 309550]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Pastore, A.]] | [[Category: Pastore, A.]] | ||
[[Category: Ramos, A.]] | [[Category: Ramos, A.]] | ||
| - | [[Category: fmrp]] | + | [[Category: fmrp,protein-protein interaction]] |
[[Category: mrna transport]] | [[Category: mrna transport]] | ||
[[Category: nuclear protein]] | [[Category: nuclear protein]] | ||
| - | [[Category: protein-protein interaction]] | ||
| - | ''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 02:07:40 2008'' |
Revision as of 23:07, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE N-TERMINAL DOMAIN OF FRAGILE X MENTAL RETARDATION PROTEIN
Overview
FMRP, whose lack of expression causes the X-linked fragile X syndrome, is a modular RNA binding protein thought to be involved in posttranslational regulation. We have solved the structure in solution of the N-terminal domain of FMRP (NDF), a functionally important region involved in multiple interactions. The structure consists of a composite fold comprising two repeats of a Tudor motif followed by a short alpha helix. The interactions between the three structural elements are essential for the stability of the NDF fold. Although structurally similar, the two repeats have different dynamic and functional properties. The second, more flexible repeat is responsible for interacting both with methylated lysine and with 82-FIP, one of the FMRP nuclear partners. NDF contains a 3D nucleolar localization signal, since destabilization of its fold leads to altered nucleolar localization of FMRP. We suggest that the NDF composite fold determines an allosteric mechanism that regulates the FMRP functions.
About this Structure
2BKD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction., Ramos A, Hollingworth D, Adinolfi S, Castets M, Kelly G, Frenkiel TA, Bardoni B, Pastore A, Structure. 2006 Jan;14(1):21-31. PMID:16407062
Page seeded by OCA on Mon Mar 31 02:07:40 2008
