4cg4

From Proteopedia

(Difference between revisions)

Revision as of 17:44, 7 September 2022

Crystal structure of the CHS-B30.2 domains of TRIM20

Structural highlights

4cg4 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[MEFV_HUMAN] Defects in MEFV are the cause of familial Mediterranean fever autosomal recessive (ARFMF) [MIM:249100]. ARFMF is an inherited disorder characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. ARFMF is frequently complicated by amyloidosis, which leads to renal failure and can be prophylactically treated with colchicine. ARFMF primarily affects ancestral ethnic groups living around the Mediterranean basin: North African Jews, Armenians, Arabs and Turks. The disease is also distributed in other populations including Greeks, Cypriots, Italians and Spanish, although at a lower prevalence.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11] ^[12] ^[13] ^[14] ^[15] Defects in MEFV are the cause of familial Mediterranean fever autosomal dominant (ADFMF) [MIM:134610]. ADFMF is characterized by periodic fever, serosal inflammation and pain in the abdomen, chest or joints as seen also in the autosomal recessive form of the disease. It is associated with renal amyloidosis and characterized by colchicine unresponsiveness.

Function

[MEFV_HUMAN] Probably controls the inflammatory response in myelomonocytic cells at the level of the cytoskeleton organization.^[16] ^[17]

References

↑ . Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. The International FMF Consortium. Cell. 1997 Aug 22;90(4):797-807. PMID:9288758
↑ . A candidate gene for familial Mediterranean fever. Nat Genet. 1997 Sep;17(1):25-31. PMID:9288094 doi:10.1038/ng0997-25
↑ Timmann C, Muntau B, Kuhne K, Gelhaus A, Horstmann RD. Two novel mutations R653H and E230K in the Mediterranean fever gene associated with disease. Mutat Res. 2001 Aug 8;479(1-2):235-9. PMID:11470495
↑ Notarnicola C, Didelot MN, Kone-Paut I, Seguret F, Demaille J, Touitou I. Reduced MEFV messenger RNA expression in patients with familial Mediterranean fever. Arthritis Rheum. 2002 Oct;46(10):2785-93. PMID:12384939 doi:10.1002/art.10575
↑ Bernot A, da Silva C, Petit JL, Cruaud C, Caloustian C, Castet V, Ahmed-Arab M, Dross C, Dupont M, Cattan D, Smaoui N, Dode C, Pecheux C, Nedelec B, Medaxian J, Rozenbaum M, Rosner I, Delpech M, Grateau G, Demaille J, Weissenbach J, Touitou I. Non-founder mutations in the MEFV gene establish this gene as the cause of familial Mediterranean fever (FMF). Hum Mol Genet. 1998 Aug;7(8):1317-25. PMID:9668175
↑ Booth DR, Gillmore JD, Booth SE, Pepys MB, Hawkins PN. Pyrin/marenostrin mutations in familial Mediterranean fever. QJM. 1998 Sep;91(9):603-6. PMID:10024914
↑ Aksentijevich I, Torosyan Y, Samuels J, Centola M, Pras E, Chae JJ, Oddoux C, Wood G, Azzaro MP, Palumbo G, Giustolisi R, Pras M, Ostrer H, Kastner DL. Mutation and haplotype studies of familial Mediterranean fever reveal new ancestral relationships and evidence for a high carrier frequency with reduced penetrance in the Ashkenazi Jewish population. Am J Hum Genet. 1999 Apr;64(4):949-62. PMID:10090880
↑ Cazeneuve C, Sarkisian T, Pecheux C, Dervichian M, Nedelec B, Reinert P, Ayvazyan A, Kouyoumdjian JC, Ajrapetyan H, Delpech M, Goossens M, Dode C, Grateau G, Amselem S. MEFV-Gene analysis in armenian patients with Familial Mediterranean fever: diagnostic value and unfavorable renal prognosis of the M694V homozygous genotype-genetic and therapeutic implications. Am J Hum Genet. 1999 Jul;65(1):88-97. PMID:10364520 doi:S0002-9297(07)63731-8
↑ Shohat M, Magal N, Shohat T, Chen X, Dagan T, Mimouni A, Danon Y, Lotan R, Ogur G, Sirin A, Schlezinger M, Halpern GJ, Schwabe A, Kastner D, Rotter JI, Fischel-Ghodsian N. Phenotype-genotype correlation in familial Mediterranean fever: evidence for an association between Met694Val and amyloidosis. Eur J Hum Genet. 1999 Apr;7(3):287-92. PMID:10234504 doi:10.1038/sj.ejhg.5200303
↑ Akar N, Misiroglu M, Yalcinkaya F, Akar E, Cakar N, Tumer N, Akcakus M, Tastan H, Matzner Y. MEFV mutations in Turkish patients suffering from Familial Mediterranean Fever. Hum Mutat. 2000 Jan;15(1):118-9. PMID:10612841 doi:<118::AID-HUMU29>3.0.CO;2-5 10.1002/(SICI)1098-1004(200001)15:1<118::AID-HUMU29>3.0.CO;2-5
↑ Domingo C, Touitou I, Bayou A, Ozen S, Notarnicola C, Dewalle M, Demaille J, Buades R, Sayadat C, Levy M, Ben-Chetrit E. Familial Mediterranean fever in the 'Chuetas' of Mallorca: a question of Jewish origin or genetic heterogeneity. Eur J Hum Genet. 2000 Apr;8(4):242-6. PMID:10854105 doi:10.1038/sj.ejhg.5200462
↑ Dode C, Pecheux C, Cazeneuve C, Cattan D, Dervichian M, Goossens M, Delpech M, Amselem S, Grateau G. Mutations in the MEFV gene in a large series of patients with a clinical diagnosis of familial Mediterranean fever. Am J Med Genet. 2000 Jun 5;92(4):241-6. PMID:10842288
↑ Aldea A, Calafell F, Arostegui JI, Lao O, Rius J, Plaza S, Maso M, Vives J, Buades J, Yague J. The west side story: MEFV haplotype in Spanish FMF patients and controls, and evidence of high LD and a recombination "hot-spot" at the MEFV locus. Hum Mutat. 2004 Apr;23(4):399. PMID:15024744 doi:10.1002/humu.9229
↑ Medlej-Hashim M, Serre JL, Corbani S, Saab O, Jalkh N, Delague V, Chouery E, Salem N, Loiselet J, Lefranc G, Megarbane A. Familial Mediterranean fever (FMF) in Lebanon and Jordan: a population genetics study and report of three novel mutations. Eur J Med Genet. 2005 Oct-Dec;48(4):412-20. Epub 2005 Jun 20. PMID:16378925 doi:S1769-7212(05)00104-7
↑ Goulielmos GN, Fragouli E, Aksentijevich I, Sidiropoulos P, Boumpas DT, Eliopoulos E. Mutational analysis of the PRYSPRY domain of pyrin and implications for familial mediterranean fever (FMF). Biochem Biophys Res Commun. 2006 Jul 14;345(4):1326-32. Epub 2006 May 15. PMID:16730661 doi:S0006-291X(06)01029-1
↑ Centola M, Wood G, Frucht DM, Galon J, Aringer M, Farrell C, Kingma DW, Horwitz ME, Mansfield E, Holland SM, O'Shea JJ, Rosenberg HF, Malech HL, Kastner DL. The gene for familial Mediterranean fever, MEFV, is expressed in early leukocyte development and is regulated in response to inflammatory mediators. Blood. 2000 May 15;95(10):3223-31. PMID:10807793
↑ Mansfield E, Chae JJ, Komarow HD, Brotz TM, Frucht DM, Aksentijevich I, Kastner DL. The familial Mediterranean fever protein, pyrin, associates with microtubules and colocalizes with actin filaments. Blood. 2001 Aug 1;98(3):851-9. PMID:11468188

1 Structural highlights
2 Disease
3 Function
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cg4"

@@ Line 3: / Line 3: @@
 <StructureSection load='4cg4' size='340' side='right'caption='[[4cg4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4cg4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4cg4]] is a 6 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=4CG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CG4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DHL:2-AMINO-ETHANETHIOL'>DHL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DHL:2-AMINO-ETHANETHIOL'>DHL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></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=4cg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg4 OCA], [https://pdbe.org/4cg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cg4 RCSB], [https://www.ebi.ac.uk/pdbsum/4cg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg4 ProSAT]</span></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=4cg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg4 OCA], [http://pdbe.org/4cg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cg4 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg4 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/MEFV_HUMAN MEFV_HUMAN]] Defects in MEFV are the cause of familial Mediterranean fever autosomal recessive (ARFMF) [MIM:[http://omim.org/entry/249100 249100]]. ARFMF is an inherited disorder characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. ARFMF is frequently complicated by amyloidosis, which leads to renal failure and can be prophylactically treated with colchicine. ARFMF primarily affects ancestral ethnic groups living around the Mediterranean basin: North African Jews, Armenians, Arabs and Turks. The disease is also distributed in other populations including Greeks, Cypriots, Italians and Spanish, although at a lower prevalence.<ref>PMID:9288758</ref> <ref>PMID:9288094</ref> <ref>PMID:11470495</ref> <ref>PMID:12384939</ref> <ref>PMID:9668175</ref> <ref>PMID:10024914</ref> <ref>PMID:10090880</ref> <ref>PMID:10364520</ref> <ref>PMID:10234504</ref> <ref>PMID:10612841</ref> <ref>PMID:10854105</ref> <ref>PMID:10842288</ref> <ref>PMID:15024744</ref> <ref>PMID:16378925</ref> <ref>PMID:16730661</ref>   Defects in MEFV are the cause of familial Mediterranean fever autosomal dominant (ADFMF) [MIM:[http://omim.org/entry/134610 134610]]. ADFMF is characterized by periodic fever, serosal inflammation and pain in the abdomen, chest or joints as seen also in the autosomal recessive form of the disease. It is associated with renal amyloidosis and characterized by colchicine unresponsiveness.
+[[https://www.uniprot.org/uniprot/MEFV_HUMAN MEFV_HUMAN]] Defects in MEFV are the cause of familial Mediterranean fever autosomal recessive (ARFMF) [MIM:[https://omim.org/entry/249100 249100]]. ARFMF is an inherited disorder characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. ARFMF is frequently complicated by amyloidosis, which leads to renal failure and can be prophylactically treated with colchicine. ARFMF primarily affects ancestral ethnic groups living around the Mediterranean basin: North African Jews, Armenians, Arabs and Turks. The disease is also distributed in other populations including Greeks, Cypriots, Italians and Spanish, although at a lower prevalence.<ref>PMID:9288758</ref> <ref>PMID:9288094</ref> <ref>PMID:11470495</ref> <ref>PMID:12384939</ref> <ref>PMID:9668175</ref> <ref>PMID:10024914</ref> <ref>PMID:10090880</ref> <ref>PMID:10364520</ref> <ref>PMID:10234504</ref> <ref>PMID:10612841</ref> <ref>PMID:10854105</ref> <ref>PMID:10842288</ref> <ref>PMID:15024744</ref> <ref>PMID:16378925</ref> <ref>PMID:16730661</ref>   Defects in MEFV are the cause of familial Mediterranean fever autosomal dominant (ADFMF) [MIM:[https://omim.org/entry/134610 134610]]. ADFMF is characterized by periodic fever, serosal inflammation and pain in the abdomen, chest or joints as seen also in the autosomal recessive form of the disease. It is associated with renal amyloidosis and characterized by colchicine unresponsiveness.
 == Function ==
-[[http://www.uniprot.org/uniprot/MEFV_HUMAN MEFV_HUMAN]] Probably controls the inflammatory response in myelomonocytic cells at the level of the cytoskeleton organization.<ref>PMID:10807793</ref> <ref>PMID:11468188</ref>
+[[https://www.uniprot.org/uniprot/MEFV_HUMAN MEFV_HUMAN]] Probably controls the inflammatory response in myelomonocytic cells at the level of the cytoskeleton organization.<ref>PMID:10807793</ref> <ref>PMID:11468188</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Many tripartite motif-containing (TRIM) proteins, comprising RING-finger, B-Box, and coiled-coil domains, carry additional B30.2 domains on the C-terminus of the TRIM motif and are considered to be pattern recognition receptors involved in the detection of higher order oligomers (e.g. viral capsid proteins). To investigate the spatial architecture of domains in TRIM proteins we determined the crystal structure of the TRIM20Delta413 fragment at 2.4 A resolution. This structure comprises the central helical scaffold (CHS) and C-terminal B30.2 domains and reveals an anti-parallel arrangement of CHS domains placing the B-box domains 170 A apart from each other. Small-angle X-ray scattering confirmed that the linker between CHS and B30.2 domains is flexible in solution. The crystal structure suggests an interaction between the B30.2 domain and an extended stretch in the CHS domain, which involves residues that are mutated in the inherited disease Familial Mediterranean Fever. Dimerization of B30.2 domains by means of the CHS domain is crucial for TRIM20 to bind pro-IL-1beta in vitro. To exemplify how TRIM proteins could be involved in binding higher order oligomers we discuss three possible models for the TRIM5alpha/HIV-1 capsid interaction assuming different conformations of B30.2 domains.
-Crystal structure of TRIM20 C-terminal coiled-coil/B30.2 fragment: implications for the recognition of higher order oligomers.,Weinert C, Morger D, Djekic A, Grutter MG, Mittl PR Sci Rep. 2015 Jun 4;5:10819. doi: 10.1038/srep10819. PMID:26043233<ref>PMID:26043233</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4cg4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Djekic, A]]
+[[Category: Djekic A]]
-[[Category: Gruetter, M G]]
+[[Category: Gruetter MG]]
-[[Category: Mittl, P R.E]]
+[[Category: Mittl PRE]]
-[[Category: Morger, D]]
+[[Category: Morger D]]
-[[Category: Weinert, C]]
+[[Category: Weinert C]]
-[[Category: Actin-binding protein]]
-[[Category: Familial mediterranean fever]]

4cg4

From Proteopedia

Revision as of 17:44, 7 September 2022

Crystal structure of the CHS-B30.2 domains of TRIM20

Structural highlights

Disease

Function

References

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