S100 protein

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<StructureSection load='2rgi' size='350' side='right' scene='' caption='Human S-100A2 complex with isopropanol and Na+ ion (PDB code [[2rgi]])'>
<StructureSection load='2rgi' size='350' side='right' scene='' caption='Human S-100A2 complex with isopropanol and Na+ ion (PDB code [[2rgi]])'>
== Function ==
== Function ==
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S100A16 is a special member of the S100 class of calcium binding proteins, because it <scene name='Journal:JBIC:3/As/12'>performs a conformational change upon calcium(II) binding</scene> much smaller than experienced by most S100 proteins. This was observed after determination of the solution structures of apo and <scene name='Journal:JBIC:3/Dual_binding_calcium/3'>calcium(II)-bound S100A16</scene> and the <scene name='Journal:JBIC:3/Crysal/2'>crystal structure of apo S100A16</scene>. The likely reason for minimal conformational change <scene name='Journal:JBIC:3/Calcium_binding_start/7'>in S100A16</scene> is the lower calcium binding affinity and stronger <scene name='Journal:JBIC:3/Hydrophobic_interactions_2/3'>hydrophobic interaction</scene> between <scene name='Journal:JBIC:3/Please_work/3'>helix III and IV present in this protein </scene> with respect to other S100 proteins. Another characteristic of <scene name='Journal:JBIC:3/Opening/3'>S100A16</scene> is that the helix IV has the same length in <scene name='Journal:JBIC:3/25_residue_long_apo/3'>both apo</scene> and <scene name='Journal:JBIC:3/25_residue_calclium_bound/3'>calcium(II) forms</scene> because of <scene name='Journal:JBIC:3/Motif_good/5'>the presence of a Gly-Gly-Ile-Thr-Gly-Pro sequence motif</scene> in helix IV. Based on the available structures of S100 members, we analyzed and summarized all their conformational changes due to calcium(II) binding by a principal component analysis. <scene name='Journal:JBIC:3/Calcium_binding_start/7'>Calcium binding</scene> was proved by both NMR titration and Isothermal Titration Calorimetry (ITC) experiments. Even if the <scene name='Journal:JBIC:3/Binding_calcium_glu/2'>important Glu residue</scene> in the last position of first EF-hand calcium binding loop <scene name='Journal:JBIC:3/Binding_calcium/13'>is missing</scene>, these experimental data indicated that S100A16 can still bind one calcium(II) ion in such loop. NMR relaxation <scene name='Journal:JBIC:3/Flexible_broadwide/4'>studies showed that the first calcium binding loop and the beginning of the second helix</scene> are the most <scene name='Journal:JBIC:3/Flexible_broad/3'>flexible regions in both the apo and calcium(II)-bound S100A16</scene>. Although the biological function of S100A16 is still unclear yet, these structural and dynamic properties can provide useful information for further functional studies.
S100A16 is a special member of the S100 class of calcium binding proteins, because it <scene name='Journal:JBIC:3/As/12'>performs a conformational change upon calcium(II) binding</scene> much smaller than experienced by most S100 proteins. This was observed after determination of the solution structures of apo and <scene name='Journal:JBIC:3/Dual_binding_calcium/3'>calcium(II)-bound S100A16</scene> and the <scene name='Journal:JBIC:3/Crysal/2'>crystal structure of apo S100A16</scene>. The likely reason for minimal conformational change <scene name='Journal:JBIC:3/Calcium_binding_start/7'>in S100A16</scene> is the lower calcium binding affinity and stronger <scene name='Journal:JBIC:3/Hydrophobic_interactions_2/3'>hydrophobic interaction</scene> between <scene name='Journal:JBIC:3/Please_work/3'>helix III and IV present in this protein </scene> with respect to other S100 proteins. Another characteristic of <scene name='Journal:JBIC:3/Opening/3'>S100A16</scene> is that the helix IV has the same length in <scene name='Journal:JBIC:3/25_residue_long_apo/3'>both apo</scene> and <scene name='Journal:JBIC:3/25_residue_calclium_bound/3'>calcium(II) forms</scene> because of <scene name='Journal:JBIC:3/Motif_good/5'>the presence of a Gly-Gly-Ile-Thr-Gly-Pro sequence motif</scene> in helix IV. Based on the available structures of S100 members, we analyzed and summarized all their conformational changes due to calcium(II) binding by a principal component analysis. <scene name='Journal:JBIC:3/Calcium_binding_start/7'>Calcium binding</scene> was proved by both NMR titration and Isothermal Titration Calorimetry (ITC) experiments. Even if the <scene name='Journal:JBIC:3/Binding_calcium_glu/2'>important Glu residue</scene> in the last position of first EF-hand calcium binding loop <scene name='Journal:JBIC:3/Binding_calcium/13'>is missing</scene>, these experimental data indicated that S100A16 can still bind one calcium(II) ion in such loop. NMR relaxation <scene name='Journal:JBIC:3/Flexible_broadwide/4'>studies showed that the first calcium binding loop and the beginning of the second helix</scene> are the most <scene name='Journal:JBIC:3/Flexible_broad/3'>flexible regions in both the apo and calcium(II)-bound S100A16</scene>. Although the biological function of S100A16 is still unclear yet, these structural and dynamic properties can provide useful information for further functional studies.
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</StructureSection>
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== 3D Structures of S100 proteins ==
== 3D Structures of S100 proteins ==
 +
[[S100 proteins 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*S100-A1
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**[[1k2h]] – rCBP-1 – rat - NMR <br />
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**[[2k2f]] – rCBP-1 + Ca + ryanodine receptor peptide - NMR<br />
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-
**[[2kbm]] – rCBP-1 + F-actin capping protein peptide - NMR<br />
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**[[1zfs]], [[2lp2]] – hCBP-1 + Ca – human - NMR<br />
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**[[2l0p]], [[2lp3]] – hCBP-1 + Ca - NMR<br />
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**[[2lux]] - hCBP-1 (mutant) + Ca - NMR<br />
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**[[2lhl]], [[2lls]], [[2m3w]] – hCBP-1 (mutant) - NMR<br />
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**[[2llt]], [[2llu]] – hCBP-1 - NMR<br />
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**[[2jpt]] – bCBP-1 (mutant) – bovine - NMR <br />
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*S100-A2
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**[[2rgi]] – hCBP-2<br />
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**[[4duq]] – hCBP-2 (mutant) + Ca <br />
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*S100-A3
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**[[3psr]], [[3nsi]], [[3nso]] – hCBP-3 <br />
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**[[3nsk]], [[3nsl]] – hCBP-3 (mutant) <br />
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*S100-A4 (Metastasin, Placental calcium-binding protein, Calvasculin)
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**[[1m31]] – hCBP-4 - NMR <br />
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**[[2q91]] – hCBP-4 <br />
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**[[3c1v]], [[3cga]], [[3ko0]], [[4hsz]] – hCBP-4 + Ca <br />
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**[[3m0w]] – hCBP-4 + Ca + PCP<br />
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**[[3zwh]], [[4cfq]], [[4cfr]] – hCBP-4 (mutant) + Ca + myosin-9 peptide<br />
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**[[4eto]] – hCBP-4 + Ca + myosin-9 peptide<br />
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**[[2lnk]] – hCBP-4 + myosin-2a peptide - NMR<br />
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*S100-A5
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**[[2kax]] – hCBP-5 - NMR <br />
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**[[4dir]] – hCBP-5 + Ca <br />
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**[[2kay]] – hCBP-5 + Ca - NMR <br />
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*S100-A6 (Calcyclin)
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**[[1cnp]], [[1a03]], [[2cnp]], [[1jwd]] – raCBP-6 – rabbit - NMR<br />
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**[[2jtt]] – raCBP-6 + calcyclin-binding protein - NMR<br />
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**[[1kso]], [[1k8u]], [[1k9p]] – hCBP-6 <br />
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**[[1k96]], [[1k9k]] – hCBP-6 + Ca <br />
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**[[2m1k]] – hCBP-6 (mutant) + RAGE receptor - NMR <br />
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**[[4p2y]] – hCBP-6 + RAGE receptor + Ca + Zn <br />
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*S100-A7 (Psoriasin)
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**[[1psr]] – hCBP-7 + Ho <br />
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**[[2psr]], [[2wos]] – hCBP-7 + Zn + Ca <br />
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**[[2wnd]], [[4aqj]] – hCBP-7 (mutant) + Zn + Ca <br />
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**[[3psr]], [[2wor]] – hCBP-7 + Ca <br />
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*S100-A8 (Calgranulin-A; Migration inhibitory factor-related protein)
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**[[1mr8]] – hCBP-8 + Ca <br />
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**[[1irj]] – hCBP-9 + Ca <br />
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**[[1xk4]] – hCBP-8 (mutant) + Ca + hCBP-9 (mutant) <br />
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**[[4ggf]] – hCBP-8 + hCBP-9 + Ca + Mn <br />
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**[[4xgk]] – hCBP-8 (mutant) + hCBP-9 (mutant) + Ca + Mn <br />
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*S100-A9 (Calgranulin-B or Migration inhibitory factor-related protein 14)
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**[[1xk4]] – hCPB-9 (mutant) + hCBP-8 (mutant) + Ca <br />
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**[[4ggf]] – hCPB-9 + hCBP-8 + Ca + Mn<br />
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**[[1irj]] – hCBP-9 + Ca <br />
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*S100-A10 ( Calpaxin; P11)
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**[[1a4p]] – hCBP-10 <br />
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**[[1bt6]] – hCBP-10 + annexin II <br />
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**[[4drw]], [[4hrg]] – hCBP-10/annexin II + AHNAK peptide<br />
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**[[4ftg]] – hCBP-10 + annexin II + AHNAK peptide<br />
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**[[4hre]], [[4hrh]] – hCBP-10 + annexin II + helicase-like transcription factor<br />
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*S100-A11 (Calgizzarin)
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**[[1qls]] – CBP-11 + Ca + annexin I - pig <br />
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**[[1nsh]] – raCBP-11 - NMR<br />
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**[[2luc]] – hCBP-11 - NMR<br />
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**[[1v4z]], [[1v50]] – hCBP-11 N terminal - NMR<br />
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*S100-A12
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**[[2wcf]] – hCBP-12<br />
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**[[2m9g]] – hCBP-12 - NMR<br />
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**[[2wce]] – hCBP-12 (mutant) <br />
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**[[1e8a]], [[1gqm]] – hCBP-12 + Ca <br />
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**[[1odb]] – hCBP-12 + Cu + Ca <br />
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**[[2wc8]], [[2wcb]] – hCBP-12 + Zn <br />
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*S100-A13
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**[[2cxj]] – CBP-13 – mouse - NMR<br />
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**[[1yur]], [[1yus]] – hCBP-13 - NMR<br />
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**[[1yut]], [[1yuu]] – hCBP-13 + Ca - NMR<br />
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**[[2h2k]], [[2egd]] – hCBP-13 + Ca <br />
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**[[2k8m]] – hCBP-13 + peptide - NMR<br />
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**[[2ki4]] – hCBP-13 + heparin-binding growth factor - NMR<br />
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**[[2ki6]] – hCBP-13 + heparin-binding growth factor + synaptotagmin-1- NMR<br />
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**[[2l5x]] – hCBP-13 + interleukin-1 α - NMR<br />
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**[[2le9]] – hCBP-13 + RAGEC2 - NMR<br />
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**[[2kot]] – hCBP-13 + amlexanox - NMR<br />
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*S100-A14
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**[[2m0r]] – hCBP-14 - NMR<br />
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*S100-A15 (Koebnerisin or S100-A7A)
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**[[4aqi]] – hCBP-15 + Ca + Zn<br />
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*S100-A16 (S100-F)
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**[[2l50]] – hCBP-16 - NMR<br />
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**[[2l51]] – hCBP-16 + Ca - NMR<br />
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**[[3nxa]] – hCBP-16 <br />
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*S100B
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**[[1sym]], [[1b4c]] – rCBP – rat - NMR<br />
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**[[1qlk]], [[2k7o]] – rCBP + Ca - NMR<br />
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**[[1xyd]] – rCBP + Zn + Ca - NMR<br />
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**[[1dt7]] – rCBP + Ca + p53 peptide - NMR<br />
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**[[1mwn]] – rCBP + F-actin capping protein peptide - NMR<br />
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**[[1mq1]] – hCBP + F-actin capping protein peptide - NMR<br />
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**[[3rm1]] – bCBP + F-actin capping protein peptide + Ca<br />
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**[[1psb]] – bCBP + NDR kinase peptide - NMR<br />
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**[[3iqq]] – bCBP + TRTK12 peptide <br />
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**[[1cfp]] – bCBP (mutant) - NMR <br />
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**[[1mho]], [[3cr4]], [[3gk1]], [[3gk2]], [[3gk4]], [[3iqo]], [[3lk0]], [[3lk1]], [[3lle]], [[3rlz]] – bCBP + Ca <br />
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**[[3cr2]], [[3cr5]] – bCBP + Zn + Ca <br />
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**[[4pdz]], [[4pe0]], [[4pe1]], [[4pe4]], [[4pe7]] – bCBP + Ca + inhibitor<br />
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**[[4fqo]] – bCBP (mutant) + Ca + inhibitor<br />
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**[[1uwo]], [[2pru]] – hCBP - NMR <br />
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**[[2h61]], [[3hcm]] – hCBP + Ca <br />
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**[[4xyn]] – hCBP + Ca + RAGE peptide <br />
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**[[3czt]], [[3d0y]], [[3d10]] – hCBP + Zn + Ca <br />
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**[[2m49]] – hCBP + fibroblast growth factor 2 - NMR<br />
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*Calbindin D9k (S100G)
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**[[1clb]] – bCBP - NMR<br />
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**[[1cdn]], [[1bod]], [[1d1o]] – bCBP (mutant) - NMR <br />
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**[[4icb]], [[3icb]] – bCBP + Ca <br />
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**[[1ig5]] – bCBP + Mg <br />
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**[[1igv]] – bCBP + Mn <br />
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**[[1boc]], [[2bca]], [[2bcb]] – bCBP - NMR <br />
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**[[1ht9]] – bCBP (mutant) + Ca <br />
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**[[1qx2]] – bCBP (mutant) + Zn + Ca<br />
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**[[1b1g]] – bCBP (mutant) + Ca - NMR <br />
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**[[1kqv]], [[1ksm]], [[1n65]] – bCBP (mutant) + Lanthanide - NMR <br />
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**[[1kcy]], [[2maz]] – bCBP (mutant) - NMR <br />
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**[[1cb1]] – CBP – pig - NMR <br />
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*Calbindin D28k
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**[[2f33]], [[2g9b]] – rCBP - NMR<br />
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*S100P
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**[[1j55]] – hCBP + Ca <br />
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**[[1ozo]] – hCBP - NMR<br />
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*S100Z
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**[[2y5i]] – CBP + Ca - zebrafish <br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]
<references/>
<references/>

Current revision

Human S-100A2 complex with isopropanol and Na+ ion (PDB code 2rgi)

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References

  1. ↑ Donato R, Cannon BR, Sorci G, Riuzzi F, Hsu K, Weber DJ, Geczy CL. Functions of S100 proteins. Curr Mol Med. 2013 Jan;13(1):24-57. PMID:22834835
  2. ↑ Yao R, Lopez-Beltran A, Maclennan GT, Montironi R, Eble JN, Cheng L. Expression of S100 protein family members in the pathogenesis of bladder tumors. Anticancer Res. 2007 Sep-Oct;27(5A):3051-8. PMID:17970044
  3. ↑ Wilsmann-Theis D, Wagenpfeil J, Holzinger D, Roth J, Koch S, Schnautz S, Bieber T, Wenzel J. Among the S100 proteins, S100A12 is the most significant marker for psoriasis disease activity. J Eur Acad Dermatol Venereol. 2016 Jul;30(7):1165-70. doi: 10.1111/jdv.13269., Epub 2015 Sep 2. PMID:26333514 doi:http://dx.doi.org/10.1111/jdv.13269
  4. ↑ Zhu L, Okano S, Takahara M, Chiba T, Tu Y, Oda Y, Furue M. Expression of S100 protein family members in normal skin and sweat gland tumors. J Dermatol Sci. 2013 Jun;70(3):211-9. doi: 10.1016/j.jdermsci.2013.03.002. Epub, 2013 Mar 16. PMID:23623205 doi:http://dx.doi.org/10.1016/j.jdermsci.2013.03.002
  5. ↑ Bertini I, Borsi V, Cerofolini L, Das Gupta S, Fragai M, Luchinat C. Solution structure and dynamics of human S100A14. J Biol Inorg Chem. 2012 Nov 30. PMID:23197251 doi:10.1007/s00775-012-0963-3
  6. ↑ Babini E, Bertini I, Borsi V, Calderone V, Hu X, Luchinat C, Parigi G. Structural characterization of human S100A16, a low-affinity calcium binder. J Biol Inorg Chem. 2010 Nov 3. PMID:21046186 doi:10.1007/s00775-010-0721-3

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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