3ffn: Difference between revisions

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[[Image:3ffn.png|left|200px]]


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==Crystal structure of calcium-free human gelsolin==
The line below this paragraph, containing "STRUCTURE_3ffn", creates the "Structure Box" on the page.
<StructureSection load='3ffn' size='340' side='right'caption='[[3ffn]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3ffn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFN FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [https://pdbe.org/3ffn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [https://www.ebi.ac.uk/pdbsum/3ffn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffn ProSAT]</span></td></tr>
{{STRUCTURE_3ffn|  PDB=3ffn  |  SCENE=  }}
</table>
 
== Disease ==
===Crystal structure of calcium-free human gelsolin===
[https://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[https://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 ==
 
[https://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>
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== Evolutionary Conservation ==
The line below this paragraph, {{ABSTRACT_PUBMED_19666512}}, adds the Publication Abstract to the page
[[Image:Consurf_key_small.gif|200px|right]]
(as it appears on PubMed at http://www.pubmed.gov), where 19666512 is the PubMed ID number.
Check<jmol>
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  <jmolCheckbox>
{{ABSTRACT_PUBMED_19666512}}
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/3ffn_consurf.spt"</scriptWhenChecked>
 
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
==About this Structure==
    <text>to colour the structure by Evolutionary Conservation</text>
[[3ffn]] is a 2 chain structure of [[Gelsolin]] with 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=3FFN OCA].  
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ffn ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Gelsolin]]
*[[Gelsolin 3D structures|Gelsolin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:19666512</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Burtnick, L D.]]
[[Category: Large Structures]]
[[Category: Chumnarnsilpa, S.]]
[[Category: Burtnick LD]]
[[Category: Robinson, R C.]]
[[Category: Chumnarnsilpa S]]
[[Category: Actin]]
[[Category: Robinson RC]]
[[Category: Actin binding protein]]
[[Category: Actin capping]]
[[Category: Actin-binding]]
[[Category: Alternative initiation]]
[[Category: Amyloid]]
[[Category: Amyloidosis]]
[[Category: Ca-dependent]]
[[Category: Calcium]]
[[Category: Cytoplasm]]
[[Category: Cytoskeleton]]
[[Category: Disease mutation]]
[[Category: Disulfide bond]]
[[Category: Gelsolin]]
[[Category: Phosphoprotein]]
[[Category: Polymorphism]]
[[Category: Secreted]]

Latest revision as of 12:49, 21 February 2024

Crystal structure of calcium-free human gelsolinCrystal structure of calcium-free human gelsolin

Structural highlights

3ffn is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

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]

Function

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

3ffn, resolution 3.00Å

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