1ccd
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ccd' size='340' side='right'caption='[[1ccd]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1ccd' size='340' side='right'caption='[[1ccd]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1ccd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ccd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCD FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccd OCA], [https://pdbe.org/1ccd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ccd RCSB], [https://www.ebi.ac.uk/pdbsum/1ccd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ccd ProSAT]</span></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=1ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccd OCA], [https://pdbe.org/1ccd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ccd RCSB], [https://www.ebi.ac.uk/pdbsum/1ccd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ccd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/UTER_RAT UTER_RAT] Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ccd ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ccd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The rat Clara cell 17 kDa protein (previously referred to as the rat Clara cell 10 kDa protein) has been reported to inhibit phospholipase A2 and papain, and to also bind progesterone. It has been isolated from rat lung lavage fluid and crystallized in the space group P6(5)22. The structure has been determined to 3.0 A resolution using the molecular replacement method. Uteroglobin, whose amino acid sequence is 55.7% identical, was used as the search model. The structure was then refined using restrained least-squares and simulated annealing methods. The R-factor is 22.5%. The protein is a covalently bound dimer. Two disulfide bonds join the monomers together in an antiparallel manner such that the dimer encloses a large internal hydrophobic cavity. The hydrophobic cavity is large enough to serve as the progesterone binding site, but access to the cavity is limited. Each monomer is composed of four alpha-helices. The main-chain structure of the Clara cell protein closely resembles that of uteroglobin, but the nature of many of the exposed side-chains differ. This is true, particularly in a hypervariable region between residues 23 and 36, and in the H1H4 pocket. | ||
- | |||
- | Refined structure of rat Clara cell 17 kDa protein at 3.0 A resolution.,Umland TC, Swaminathan S, Furey W, Singh G, Pletcher J, Sax M J Mol Biol. 1992 Mar 20;224(2):441-8. PMID:1560460<ref>PMID:1560460</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1ccd" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Black rat]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Furey | + | [[Category: Rattus rattus]] |
- | [[Category: Pletcher | + | [[Category: Furey W]] |
- | [[Category: Sax | + | [[Category: Pletcher J]] |
- | [[Category: Singh | + | [[Category: Sax M]] |
- | [[Category: Swaminathan | + | [[Category: Singh G]] |
- | [[Category: Umland | + | [[Category: Swaminathan S]] |
- | + | [[Category: Umland TC]] |
Revision as of 15:38, 13 March 2024
REFINED STRUCTURE OF RAT CLARA CELL 17 KDA PROTEIN AT 3.0 ANGSTROMS RESOLUTION
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Categories: Large Structures | Rattus rattus | Furey W | Pletcher J | Sax M | Singh G | Swaminathan S | Umland TC