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[[Image:2prf.gif|left|200px]]<br /><applet load="2prf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2prf" />
'''THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I'''<br />


==Overview==
==THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I==
We have determined a medium resolution three-dimensional solution structure of Acanthamoeba profilin-I by multidimensional nuclear magnetic resonance spectroscopy. This 13-kD actin binding protein consists of a five stranded antiparallel beta sheet flanked by NH2- and COOH-terminal helices on one face and by a third helix and a two stranded beta sheet on the other face. Data from actin-profilin cross-linking experiments and the localization of conserved residues between profilins in different phyla indicate that actin binding occurs on the molecular face occupied by the terminal helices. The other face of the molecule contains the residues that differ between Acanthamoeba profilins-I and II and may be important in determining the difference in polyphosphoinositide binding between these isoforms. This suggests that lipids and actin bind to different faces of the molecule.
<StructureSection load='2prf' size='340' side='right'caption='[[2prf]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2prf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_sp. Acanthamoeba sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PRF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2prf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prf OCA], [https://pdbe.org/2prf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2prf RCSB], [https://www.ebi.ac.uk/pdbsum/2prf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2prf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRO1A_ACACA PRO1A_ACACA] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/2prf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=2prf ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2PRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_sp. Acanthamoeba sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRF OCA].
*[[Profilin 3D Structures|Profilin 3D Structures]]
 
__TOC__
==Reference==
</StructureSection>
Three-dimensional solution structure of Acanthamoeba profilin-I., Vinson VK, Archer SJ, Lattman EE, Pollard TD, Torchia DA, J Cell Biol. 1993 Sep;122(6):1277-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8397216 8397216]
[[Category: Acanthamoeba sp]]
[[Category: Acanthamoeba sp.]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Archer SJ]]
[[Category: Archer, S J.]]
[[Category: Lattman EE]]
[[Category: Lattman, E E.]]
[[Category: Pollard TD]]
[[Category: Pollard, T D.]]
[[Category: Torchia DA]]
[[Category: Torchia, D A.]]
[[Category: Vinson VK]]
[[Category: Vinson, V K.]]
[[Category: actin-binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:15 2008''

Latest revision as of 10:05, 1 May 2024

THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN ITHREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I

Structural highlights

2prf is a 1 chain structure with sequence from Acanthamoeba sp.. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRO1A_ACACA Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.

Evolutionary Conservation

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

See Also

Drag the structure with the mouse to rotate

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