1c0g: Difference between revisions
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{{STRUCTURE_1c0g| PDB=1c0g | SCENE= }} | {{STRUCTURE_1c0g| PDB=1c0g | SCENE= }} | ||
===CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)=== | |||
{{ABSTRACT_PUBMED_10669610}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[http://omim.org/entry/105120 105120]]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.<ref>PMID:2157434</ref><ref>PMID:2153578</ref><ref>PMID:2176481</ref><ref>PMID:1338910</ref> | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.<ref>PMID:20393563</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[1c0g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | [[1c0g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0G OCA]. | ||
==See Also== | ==See Also== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:010669610</ref><references group="xtra"/> | <ref group="xtra">PMID:010669610</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Tetrahymena thermophila]] | |||
[[Category: Kamiya, N.]] | [[Category: Kamiya, N.]] | ||
[[Category: Kawamoto, M.]] | [[Category: Kawamoto, M.]] |
Revision as of 21:13, 24 March 2013
CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)
Template:ABSTRACT PUBMED 10669610
DiseaseDisease
[GELS_HUMAN] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:105120]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.[1][2][3][4]
FunctionFunction
[GELS_HUMAN] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.[5]
About this StructureAbout this Structure
1c0g is a 2 chain structure with sequence from Homo sapiens and Tetrahymena thermophila. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Matsuura Y, Stewart M, Kawamoto M, Kamiya N, Saeki K, Yasunaga T, Wakabayashi T. Structural basis for the higher Ca(2+)-activation of the regulated actin-activated myosin ATPase observed with Dictyostelium/Tetrahymena actin chimeras. J Mol Biol. 2000 Feb 18;296(2):579-95. PMID:10669610 doi:http://dx.doi.org/10.1006/jmbi.1999.3467
- ↑ Haltia M, Prelli F, Ghiso J, Kiuru S, Somer H, Palo J, Frangione B. Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein. Biochem Biophys Res Commun. 1990 Mar 30;167(3):927-32. PMID:2157434
- ↑ Maury CP, Alli K, Baumann M. Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline. FEBS Lett. 1990 Jan 15;260(1):85-7. PMID:2153578
- ↑ Ghiso J, Haltia M, Prelli F, Novello J, Frangione B. Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type. Biochem J. 1990 Dec 15;272(3):827-30. PMID:2176481
- ↑ de la Chapelle A, Tolvanen R, Boysen G, Santavy J, Bleeker-Wagemakers L, Maury CP, Kere J. Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187. Nat Genet. 1992 Oct;2(2):157-60. PMID:1338910 doi:http://dx.doi.org/10.1038/ng1092-157
- ↑ Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, Ideker T, Aza-Blanc P, Gleeson JG. Functional genomic screen for modulators of ciliogenesis and cilium length. Nature. 2010 Apr 15;464(7291):1048-51. doi: 10.1038/nature08895. PMID:20393563 doi:10.1038/nature08895