1ckw: Difference between revisions

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-[[Image:1ckw.png|left|200px]]
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+==CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, THE MOST COMMON SITE OF DISEASE-CAUSING DELTA-F508 MUTATION==
-The line below this paragraph, containing "STRUCTURE_1ckw", creates the "Structure Box" on the page.
+<StructureSection load='1ckw' size='340' side='right'caption='[[1ckw]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ckw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CKW FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ckw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckw OCA], [https://pdbe.org/1ckw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ckw RCSB], [https://www.ebi.ac.uk/pdbsum/1ckw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ckw ProSAT]</span></td></tr>
-{{STRUCTURE_1ckw|  PDB=1ckw  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CFTR_SHEEP CFTR_SHEEP] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1 (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Most cases of cystic fibrosis (CF), a common inherited disease of epithelial cell origin, are caused by the deletion of Phe508 located in the first nucleotide-binding domain (NBF1) of the protein called CFTR (cystic fibrosis transmembrane conductance regulator). To gain greater insight into the structure within the Phe508 region of the wild-type protein and the change in structure that occurs when this residue is deleted, we conducted nuclear magnetic resonance (NMR) studies on representative synthetic 26 and 25 amino acid peptide segments. 2D 1H NMR studies at 600 MHz of the 26-residue peptide consisting of Met498 to Ala523 in 10% DMSO, pH 4.0, at 25 degrees C show a continuous but labile helix from Gly500 to Lys522, based on both NH-NH(i,i+1) and alphaH-NH(i,i+1) NOEs. Phe508 within this helix shows only short-range (i, &lt;/=i + 2) NOEs. The corresponding 25-residue peptide lacking Phe508 also forms a labile helix from Gly500 to Lys522. However, the relative intensities of the NH-NH(i, i+1)/alphaH-NH(i,i+1) NOEs, fewer intermediate-range NOEs, and downfield alphaH and NH chemical shifts indicate a lower helical propensity of the 25-mer between residues 505 and 517, surrounding the missing residue, Phe508. 2D 1H NMR studies of both peptides in saturating (43%) TFE reveal stable alpha-helices from Gly500 to Lys522, based on NH-NH(i,i+1,2,3), alphaH-NH(i,i+2,3,4), alphaH-betaH(i,i+3), and weak alphaH-NH(i,i+1) NOEs. However, downfield shifts of the alphaH resonances from residues Gly500 to Ile507 and fewer intermediate-range NOEs suggest a less stable alpha-helix in the 25-mer even in saturating TFE. These findings show that the Phe508-containing region of CFTR has a propensity to form an alpha-helix, which is destabilized by the DeltaF508 mutation found in most patients with CF. These studies have direct relevance to better understanding the CFTR misfolding problem associated with CF and to identifying chemical agents, which correct this problem.
-===CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, THE MOST COMMON SITE OF DISEASE-CAUSING DELTA-F508 MUTATION===
+Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.,Massiah MA, Ko YH, Pedersen PL, Mildvan AS Biochemistry. 1999 Jun 8;38(23):7453-61. PMID:10360942<ref>PMID:10360942</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_10360942}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1ckw" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 10360942 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_10360942}}
-==About this Structure==
-[[1ckw]] is a 1 chain structure of [[ABC transporter]]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKW OCA].
 ==See Also==
-*[[ABC transporter]]
+*[[ABC transporter 3D structures|ABC transporter 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:10360942</ref><references group="xtra"/>
+__TOC__
-[[Category: Ko, Y H.]]
+</StructureSection>
-[[Category: Massiah, M A.]]
+[[Category: Large Structures]]
-[[Category: Mildvan, A S.]]
+[[Category: Ovis aries]]
-[[Category: Pedersen, P L.]]
+[[Category: Ko YH]]
-[[Category: Cystic fibrosis]]
+[[Category: Massiah MA]]
-[[Category: Metal transport]]
+[[Category: Mildvan AS]]
-[[Category: Nmr]]
+[[Category: Pedersen PL]]
-[[Category: P25_tfe]]
-[[Category: Peptide]]