1onv

<StructureSection load='1onv' size='340' side='right'caption='[[1onv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1onv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ONV FirstGlance]. <br>

</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=1onv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1onv OCA], [https://pdbe.org/1onv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1onv RCSB], [https://www.ebi.ac.uk/pdbsum/1onv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1onv ProSAT]</span></td></tr>

== Disease ==

[[https://www.uniprot.org/uniprot/CTDP1_HUMAN CTDP1_HUMAN]] Defects in CTDP1 are a cause of congenital cataracts facial dysmorphism and neuropathy syndrome (CCFDN) [MIM:[https://omim.org/entry/604168 604168]]. CCFDN is an autosomal recessive developmental disorder that occurs in an endogamous group of Vlax Roma (Gypsies). The syndrome is characterized by a complex clinical phenotype with seemingly unrelated features involving multiple organs and systems. Developmental abnormalities include congenital cataracts and microcorneae, hypomyelination of the peripheral nervous system, impaired physical growth, delayed early motor and intellectual development, facial dysmorphism and hypogonadism. Central nervous system involvement, with cerebral and spinal cord atrophy, may be the result of disrupted development with superimposed degenerative changes. Affected individuals are prone to severe rhabdomyolysis after viral infections and to serious complications related to general anesthesia (such as pulmonary edema and epileptic seizures).<ref>PMID:14517542</ref>

[[https://www.uniprot.org/uniprot/T2FA_HUMAN T2FA_HUMAN]] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.<ref>PMID:10428810</ref> [[https://www.uniprot.org/uniprot/CTDP1_HUMAN CTDP1_HUMAN]] Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.<ref>PMID:22692537</ref>

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== Publication Abstract from PubMed ==

FCP1 [transcription factor IIF (TFIIF)-associated carboxyl-terminal domain (CTD) phosphatase] is the only identified phosphatase specific for the phosphorylated CTD of RNA polymerase II (RNAP II). The phosphatase activity of FCP1 is enhanced in the presence of the large subunit of TFIIF (RAP74 in humans). It has been demonstrated that the CTD of RAP74 (cterRAP74; residues 436-517) directly interacts with the highly acidic CTD of FCP1 (cterFCP; residues 879-961 in human). In this manuscript, we have determined a high-resolution solution structure of a cterRAP74cterFCP complex by NMR spectroscopy. Interestingly, the cterFCP protein is completely disordered in the unbound state, but forms an alpha-helix (H1'; E945-M961) in the complex. The cterRAP74cterFCP binding interface relies extensively on van der Waals contacts between hydrophobic residues from the H2 and H3 helices of cterRAP74 and hydrophobic residues from the H1' helix of cterFCP. The binding interface also contains two critical electrostatic interactions involving aspartic acid residues from H1' of cterFCP and lysine residues from both H2 and H3 of cterRAP74. There are also three additional polar interactions involving highly conserved acidic residues from the H1' helix. The cterRAP74cterFCP complex is the first high-resolution structure between an acidic residue-rich domain from a holoenzyme-associated regulatory protein and a general transcription factor. The structure defines a clear role for both hydrophobic and acidic residues in proteinprotein complexes involving acidic residue-rich domains in transcription regulatory proteins.

NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.,Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG Proc Natl Acad Sci U S A. 2003 May 13;100(10):5688-93. Epub 2003 May 5. PMID:12732728<ref>PMID:12732728</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1onv" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Abbott, K L]]

[[Category: Archambault, J]]

[[Category: Greenblatt, J]]

[[Category: Kobor, M S]]

[[Category: Legault, P]]

[[Category: Nguyen, B D]]

[[Category: Omichinski, J G]]

[[Category: Potempa, K]]

[[Category: Transcription factor]]