1m31: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m31]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M31 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1m31]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M31 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m31 RCSB], [http://www.ebi.ac.uk/pdbsum/1m31 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m31 RCSB], [http://www.ebi.ac.uk/pdbsum/1m31 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bresnick, A R | [[Category: Bresnick, A R]] | ||
[[Category: Ellis, K C | [[Category: Ellis, K C]] | ||
[[Category: Rustandi, R R | [[Category: Rustandi, R R]] | ||
[[Category: Vallely, K M | [[Category: Vallely, K M]] | ||
[[Category: Varlamova, O | [[Category: Varlamova, O]] | ||
[[Category: Weber, D J | [[Category: Weber, D J]] | ||
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
[[Category: Non-covalent homodimer]] | [[Category: Non-covalent homodimer]] | ||
[[Category: X-type four-helix bundle]] | [[Category: X-type four-helix bundle]] | ||
Revision as of 18:19, 5 January 2015
Three-Dimensional Solution Structure of Apo-Mts1Three-Dimensional Solution Structure of Apo-Mts1
Structural highlights
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 PubMedMts1 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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