6yel

From Proteopedia

(Difference between revisions)

Revision as of 11:08, 14 June 2023

Stromal interaction molecule 1 coiled-coil 1 fragment

Structural highlights

6yel is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

STIM1_HUMAN Defects in STIM1 are the cause of immune dysfunction with T-cell inactivation due to calcium entry defect type 2 (IDTICED2) [MIM:612783. IDTICED2 is an immune disorder characterized by recurrent infections, impaired T-cell activation and proliferative response, decreased T-cell production of cytokines, lymphadenopathy, and normal lymphocytes counts and serum immunoglobulin levels. Additional features include thrombocytopenia, autoimmune hemolytic anemia, non-progressive myopathy, partial iris hypoplasia, hepatosplenomegaly and defective enamel dentition.^[1]

Function

STIM1_HUMAN Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, TMEM142A/ORAI1.^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10]

Publication Abstract from PubMed

The calcium release activated calcium channel is activated by the endoplasmic reticulum-resident calcium sensor protein STIM1. On activation, STIM1 C terminus changes from an inactive, tight to an active, extended conformation. A coiled-coil clamp involving the CC1 and CC3 domains is essential in controlling STIM1 activation, with CC1 as the key entity. The nuclear magnetic resonance-derived solution structure of the CC1 domain represents a three-helix bundle stabilized by interhelical contacts, which are absent in the Stormorken disease-related STIM1 R304W mutant. Two interhelical sites between the CC1alpha1 and CC1alpha2 helices are key in controlling STIM1 activation, affecting the balance between tight and extended conformations. Nuclear magnetic resonance-directed mutations within these interhelical interactions restore the physiological, store-dependent activation behavior of the gain-of-function STIM1 R304W mutant. This study reveals the functional impact of interhelical interactions within the CC1 domain for modifying the CC1-CC3 clamp strength to control the activation of STIM1.

Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation.,Rathner P, Fahrner M, Cerofolini L, Grabmayr H, Horvath F, Krobath H, Gupta A, Ravera E, Fragai M, Bechmann M, Renger T, Luchinat C, Romanin C, Muller N Nat Chem Biol. 2020 Oct 26. pii: 10.1038/s41589-020-00672-8. doi:, 10.1038/s41589-020-00672-8. PMID:33106661^[11]

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

References

↑ Picard C, McCarl CA, Papolos A, Khalil S, Luthy K, Hivroz C, LeDeist F, Rieux-Laucat F, Rechavi G, Rao A, Fischer A, Feske S. STIM1 mutation associated with a syndrome of immunodeficiency and autoimmunity. N Engl J Med. 2009 May 7;360(19):1971-80. doi: 10.1056/NEJMoa0900082. PMID:19420366 doi:http://dx.doi.org/10.1056/NEJMoa0900082
↑ Sabbioni S, Barbanti-Brodano G, Croce CM, Negrini M. GOK: a gene at 11p15 involved in rhabdomyosarcoma and rhabdoid tumor development. Cancer Res. 1997 Oct 15;57(20):4493-7. PMID:9377559
↑ Liou J, Kim ML, Heo WD, Jones JT, Myers JW, Ferrell JE Jr, Meyer T. STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx. Curr Biol. 2005 Jul 12;15(13):1235-41. PMID:16005298 doi:10.1016/j.cub.2005.05.055
↑ Roos J, DiGregorio PJ, Yeromin AV, Ohlsen K, Lioudyno M, Zhang S, Safrina O, Kozak JA, Wagner SL, Cahalan MD, Velicelebi G, Stauderman KA. STIM1, an essential and conserved component of store-operated Ca2+ channel function. J Cell Biol. 2005 May 9;169(3):435-45. Epub 2005 May 2. PMID:15866891 doi:jcb.200502019
↑ Zhang SL, Yu Y, Roos J, Kozak JA, Deerinck TJ, Ellisman MH, Stauderman KA, Cahalan MD. STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane. Nature. 2005 Oct 6;437(7060):902-5. PMID:16208375 doi:nature04147
↑ Mercer JC, Dehaven WI, Smyth JT, Wedel B, Boyles RR, Bird GS, Putney JW Jr. Large store-operated calcium selective currents due to co-expression of Orai1 or Orai2 with the intracellular calcium sensor, Stim1. J Biol Chem. 2006 Aug 25;281(34):24979-90. Epub 2006 Jun 28. PMID:16807233 doi:M604589200
↑ Soboloff J, Spassova MA, Tang XD, Hewavitharana T, Xu W, Gill DL. Orai1 and STIM reconstitute store-operated calcium channel function. J Biol Chem. 2006 Jul 28;281(30):20661-5. Epub 2006 Jun 9. PMID:16766533 doi:10.1074/jbc.C600126200
↑ Peinelt C, Vig M, Koomoa DL, Beck A, Nadler MJ, Koblan-Huberson M, Lis A, Fleig A, Penner R, Kinet JP. Amplification of CRAC current by STIM1 and CRACM1 (Orai1). Nat Cell Biol. 2006 Jul;8(7):771-3. Epub 2006 May 30. PMID:16733527 doi:ncb1435
↑ Spassova MA, Soboloff J, He LP, Xu W, Dziadek MA, Gill DL. STIM1 has a plasma membrane role in the activation of store-operated Ca(2+) channels. Proc Natl Acad Sci U S A. 2006 Mar 14;103(11):4040-5. Epub 2006 Mar 6. PMID:16537481 doi:0510050103
↑ Palty R, Raveh A, Kaminsky I, Meller R, Reuveny E. SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling. Cell. 2012 Apr 13;149(2):425-38. doi: 10.1016/j.cell.2012.01.055. Epub 2012 Mar, 29. PMID:22464749 doi:10.1016/j.cell.2012.01.055
↑ Rathner P, Fahrner M, Cerofolini L, Grabmayr H, Horvath F, Krobath H, Gupta A, Ravera E, Fragai M, Bechmann M, Renger T, Luchinat C, Romanin C, Muller N. Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation. Nat Chem Biol. 2020 Oct 26. pii: 10.1038/s41589-020-00672-8. doi:, 10.1038/s41589-020-00672-8. PMID:33106661 doi:http://dx.doi.org/10.1038/s41589-020-00672-8

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6yel"

@@ Line 1: / Line 1: @@
 ==Stromal interaction molecule 1 coiled-coil 1 fragment==
-<StructureSection load='6yel' size='340' side='right'caption='[[6yel]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6yel' size='340' side='right'caption='[[6yel]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6yel]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YEL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YEL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6yel]] is a 1 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=6YEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YEL FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STIM1, GOK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=6yel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yel OCA], [https://pdbe.org/6yel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yel RCSB], [https://www.ebi.ac.uk/pdbsum/6yel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yel ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yel OCA], [http://pdbe.org/6yel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yel RCSB], [http://www.ebi.ac.uk/pdbsum/6yel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yel ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/STIM1_HUMAN STIM1_HUMAN]] Defects in STIM1 are the cause of immune dysfunction with T-cell inactivation due to calcium entry defect type 2 (IDTICED2) [MIM:[http://omim.org/entry/612783 612783]]. IDTICED2 is an immune disorder characterized by recurrent infections, impaired T-cell activation and proliferative response, decreased T-cell production of cytokines, lymphadenopathy, and normal lymphocytes counts and serum immunoglobulin levels. Additional features include thrombocytopenia, autoimmune hemolytic anemia, non-progressive myopathy, partial iris hypoplasia, hepatosplenomegaly and defective enamel dentition.<ref>PMID:19420366</ref>
+[https://www.uniprot.org/uniprot/STIM1_HUMAN STIM1_HUMAN] Defects in STIM1 are the cause of immune dysfunction with T-cell inactivation due to calcium entry defect type 2 (IDTICED2) [MIM:[https://omim.org/entry/612783 612783]. IDTICED2 is an immune disorder characterized by recurrent infections, impaired T-cell activation and proliferative response, decreased T-cell production of cytokines, lymphadenopathy, and normal lymphocytes counts and serum immunoglobulin levels. Additional features include thrombocytopenia, autoimmune hemolytic anemia, non-progressive myopathy, partial iris hypoplasia, hepatosplenomegaly and defective enamel dentition.<ref>PMID:19420366</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/STIM1_HUMAN STIM1_HUMAN]] Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, TMEM142A/ORAI1.<ref>PMID:9377559</ref> <ref>PMID:16005298</ref> <ref>PMID:15866891</ref> <ref>PMID:16208375</ref> <ref>PMID:16807233</ref> <ref>PMID:16766533</ref> <ref>PMID:16733527</ref> <ref>PMID:16537481</ref> <ref>PMID:22464749</ref>
+[https://www.uniprot.org/uniprot/STIM1_HUMAN STIM1_HUMAN] Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, TMEM142A/ORAI1.<ref>PMID:9377559</ref> <ref>PMID:16005298</ref> <ref>PMID:15866891</ref> <ref>PMID:16208375</ref> <ref>PMID:16807233</ref> <ref>PMID:16766533</ref> <ref>PMID:16733527</ref> <ref>PMID:16537481</ref> <ref>PMID:22464749</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bechmann, M]]
+[[Category: Bechmann M]]
-[[Category: Cerofolini, L]]
+[[Category: Cerofolini L]]
-[[Category: Fahrner, M]]
+[[Category: Fahrner M]]
-[[Category: Fragai, M]]
+[[Category: Fragai M]]
-[[Category: Grabmayr, H]]
+[[Category: Grabmayr H]]
-[[Category: Luchinat, C]]
+[[Category: Luchinat C]]
-[[Category: Mueller, N]]
+[[Category: Mueller N]]
-[[Category: Rathner, P]]
+[[Category: Rathner P]]
-[[Category: Ravera, E]]
+[[Category: Ravera E]]
-[[Category: Romanin, C]]
+[[Category: Romanin C]]
-[[Category: Calcium signaling]]
-[[Category: Crac]]
-[[Category: Signaling protein]]
-[[Category: Store-operated ca2+ entry]]

6yel

From Proteopedia

Revision as of 11:08, 14 June 2023

Stromal interaction molecule 1 coiled-coil 1 fragment

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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