3c1v: Difference between revisions

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[[Image:3c1v.jpg|left|200px]]


<!--
==The 1.5 A Crystal structure of Ca2+-bound S100A4==
The line below this paragraph, containing "STRUCTURE_3c1v", creates the "Structure Box" on the page.
<StructureSection load='3c1v' size='340' side='right'caption='[[3c1v]], [[Resolution|resolution]] 1.50&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'>[[3c1v]] is a 4 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=3C1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C1V 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]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
{{STRUCTURE_3c1v|  PDB=3c1v  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1v OCA], [https://pdbe.org/3c1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c1v RCSB], [https://www.ebi.ac.uk/pdbsum/3c1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S10A4_HUMAN S10A4_HUMAN]
== 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/c1/3c1v_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=3c1v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
S100A4 takes part in control of tumour cell migration and contributes to metastatic spread in in vivo models. In the active dimeric Ca(2+)-bound state it interacts with multiple intracellular targets. Conversely, oligomeric forms of S100A4 are linked with the extracellular function of this protein. We report the 1.5A X-ray crystal structure of Ca(2+)-bound S100A4 and use it to identify the residues involved in target recognition and to derive a model of the oligomeric state. We applied stopped-flow analysis of tyrosine fluorescence to derive kinetics of S100A4 activation by Ca(2+) (k(on)=3.5 microM(-1)s(-1), k(off)=20s(-1)).


'''The 1.5 A Crystal structure of Ca2+-bound S100A4'''
Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4.,Gingras AR, Basran J, Prescott A, Kriajevska M, Bagshaw CR, Barsukov IL FEBS Lett. 2008 May 28;582(12):1651-6. Epub 2008 Apr 22. PMID:18435928<ref>PMID:18435928</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3c1v" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
S100A4 takes part in control of tumour cell migration and contributes to metastatic spread in in vivo models. In the active dimeric Ca(2+)-bound state it interacts with multiple intracellular targets. Conversely, oligomeric forms of S100A4 are linked with the extracellular function of this protein. We report the 1.5A X-ray crystal structure of Ca(2+)-bound S100A4 and use it to identify the residues involved in target recognition and to derive a model of the oligomeric state. We applied stopped-flow analysis of tyrosine fluorescence to derive kinetics of S100A4 activation by Ca(2+) (k(on)=3.5muM(-1)s(-1), k(off)=20s(-1)).
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
 
== References ==
==About this Structure==
<references/>
3C1V is a [[Single protein]] structure of 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=3C1V OCA].
__TOC__
 
</StructureSection>
==Reference==
Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4., Gingras AR, Basran J, Prescott A, Kriajevska M, Bagshaw CR, Barsukov IL, FEBS Lett. 2008 May 28;582(12):1651-6. Epub 2008 Apr 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18435928 18435928]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Barsukov, I L.]]
[[Category: Barsukov IL]]
[[Category: Gingras, A R.]]
[[Category: Gingras AR]]
[[Category: Ca2+-bound]]
[[Category: Calcium binding protein]]
[[Category: Calcium-bound]]
[[Category: S100a4]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun  4 10:01:51 2008''

Latest revision as of 17:54, 1 November 2023

The 1.5 A Crystal structure of Ca2+-bound S100A4The 1.5 A Crystal structure of Ca2+-bound S100A4

Structural highlights

3c1v is a 4 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 1.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

S10A4_HUMAN

Evolutionary Conservation

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

Publication Abstract from PubMed

S100A4 takes part in control of tumour cell migration and contributes to metastatic spread in in vivo models. In the active dimeric Ca(2+)-bound state it interacts with multiple intracellular targets. Conversely, oligomeric forms of S100A4 are linked with the extracellular function of this protein. We report the 1.5A X-ray crystal structure of Ca(2+)-bound S100A4 and use it to identify the residues involved in target recognition and to derive a model of the oligomeric state. We applied stopped-flow analysis of tyrosine fluorescence to derive kinetics of S100A4 activation by Ca(2+) (k(on)=3.5 microM(-1)s(-1), k(off)=20s(-1)).

Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4.,Gingras AR, Basran J, Prescott A, Kriajevska M, Bagshaw CR, Barsukov IL FEBS Lett. 2008 May 28;582(12):1651-6. Epub 2008 Apr 22. PMID:18435928[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Gingras AR, Basran J, Prescott A, Kriajevska M, Bagshaw CR, Barsukov IL. Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4. FEBS Lett. 2008 May 28;582(12):1651-6. Epub 2008 Apr 22. PMID:18435928 doi:10.1016/j.febslet.2008.04.017

3c1v, resolution 1.50Å

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