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New page: left|200px<br /> <applet load="1m31" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m31" /> '''Three-Dimensional Solution Structure of Apo...
 
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[[Image:1m31.gif|left|200px]]<br />
<applet load="1m31" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m31" />
'''Three-Dimensional Solution Structure of Apo-Mts1'''<br />


==Overview==
==Three-Dimensional Solution Structure of Apo-Mts1==
Mts1 is a member of the S100 family of Ca2+-binding proteins and is, implicated in promoting tumor progression and metastasis. To better, understand the structure-function relationships of this protein and to, begin characterizing its Ca2+-dependent interaction with protein binding, targets, the three-dimensional structure of mts1 was determined in the apo, state by NMR spectroscopy. As with other S100 protein family members, mts1, is a symmetric homodimer held together by noncovalent interactions between, two helices from each subunit (helices 1, 4, 1', and 4') to form an X-type, four-helix bundle. Each subunit of mts1 has two EF-hand Ca2+-binding, domains: a pseudo-EF-hand (or S100-hand) and a typical EF-hand that are, brought into proximity by a small two-stranded antiparallel beta-sheet., The S100-hand is formed by helices 1 and 2, and is similar in conformation, to other members of the S100 family. In the typical EF-hand, the position, of helix 3 is similar to that of another member of the S100 protein, family, calcyclin (S100A6), and less like that of other S100 family, members for which three-dimensional structures are available in the, calcium-free state (e.g., S100B and S100A1). The differences in the, position of helix 3 in the apo state of these four S100 proteins are, likely due to variations in the amino acid sequence in the C-terminus of, helix 4 and in loop 2 (the hinge region) and could potentially be used to, subclassify the S100 protein family.
<StructureSection load='1m31' size='340' side='right'caption='[[1m31]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m31]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M31 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=1m31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m31 OCA], [https://pdbe.org/1m31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m31 RCSB], [https://www.ebi.ac.uk/pdbsum/1m31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m31 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/m3/1m31_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=1m31 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mts1 is a member of the S100 family of Ca2+-binding proteins and is implicated in promoting tumor progression and metastasis. To better understand the structure-function relationships of this protein and to begin characterizing its Ca2+-dependent interaction with protein binding targets, the three-dimensional structure of mts1 was determined in the apo state by NMR spectroscopy. As with other S100 protein family members, mts1 is a symmetric homodimer held together by noncovalent interactions between two helices from each subunit (helices 1, 4, 1', and 4') to form an X-type four-helix bundle. Each subunit of mts1 has two EF-hand Ca2+-binding domains: a pseudo-EF-hand (or S100-hand) and a typical EF-hand that are brought into proximity by a small two-stranded antiparallel beta-sheet. The S100-hand is formed by helices 1 and 2, and is similar in conformation to other members of the S100 family. In the typical EF-hand, the position of helix 3 is similar to that of another member of the S100 protein family, calcyclin (S100A6), and less like that of other S100 family members for which three-dimensional structures are available in the calcium-free state (e.g., S100B and S100A1). The differences in the position of helix 3 in the apo state of these four S100 proteins are likely due to variations in the amino acid sequence in the C-terminus of helix 4 and in loop 2 (the hinge region) and could potentially be used to subclassify the S100 protein family.


==About this Structure==
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy.,Vallely KM, Rustandi RR, Ellis KC, Varlamova O, Bresnick AR, Weber DJ Biochemistry. 2002 Oct 22;41(42):12670-80. PMID:12379109<ref>PMID:12379109</ref>
1M31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M31 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy., Vallely KM, Rustandi RR, Ellis KC, Varlamova O, Bresnick AR, Weber DJ, Biochemistry. 2002 Oct 22;41(42):12670-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12379109 12379109]
</div>
<div class="pdbe-citations 1m31" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bresnick, A.R.]]
[[Category: Bresnick AR]]
[[Category: Ellis, K.C.]]
[[Category: Ellis KC]]
[[Category: Rustandi, R.R.]]
[[Category: Rustandi RR]]
[[Category: Vallely, K.M.]]
[[Category: Vallely KM]]
[[Category: Varlamova, O.]]
[[Category: Varlamova O]]
[[Category: Weber, D.J.]]
[[Category: Weber DJ]]
[[Category: non-covalent homodimer]]
[[Category: x-type four-helix bundle]]
 
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