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https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Camille+Mathieu Proteopedia - User contributions [en] 2026-10-05T07:13:32Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2525562 Sandbox Reserved 1121 2016-01-28T15:20:23Z

<p>Camille Mathieu: </p> <hr /> <div><Structure load='1B09' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <br /> Human C-Reactive Protein (CRP) is an acute phase protein belonging to the highly conserved pentraxin protein family, like as its homologue, the Serum Amyloid P component (SAP) <ref name="Thompson">PMID: 10368284</ref>. Although it is a normal serum protein, its circulating concentration raises rapidly and extensively in a cytokine-mediated in response to an infection, an inflammation or a tissue injury. In this way, serum CRP rate is empirically dose to detect many human disease <ref name="Thompson"/>. CRP was named this way because it was found that the protein could precipitate the "C" polysaccharide derived from Streptococcus pneumoniae cell wall <ref>PMID: 15337754</ref><ref name="kumar">PMID: 21541851</ref>.<br /> <br /> <br /> <br /> == Structure ==<br /> === CRP structure ===<br /> <br /> The crystal structure of CRP was determined by using SAP as the search model <ref name="Thompson"/>. The structure of CRP has been determined by X-ray crystallography at 3 Å resolution. Like SAP, the protein consists of five protomers, uncovalently bonded and nonglycosylated that are arranged symmetrically around a central pore <ref name="Volanakis">PMID: 11532280</ref>. Each subunit is a 25 kDa protein consisting of 224 residues <ref name="uniprot">[http://www.uniprot.org/uniprot/P02741 UniProtKB - P02741 (CRP_HUMAN)]</ref>. The diameter of the CRP pentamer is 102 Å, the inner pore diameter is 30 Å and the diameter of a subunit is 36 Å <ref name="agrawal">PMID: 19799114 </ref><ref name="Volanakis"/>.Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP <ref name="kumar"/>.<br /> <br /> Each subunit consist of two antiparallel <scene name='71/719862/Sheet/1'>β-sheets</scene> <ref name="uniprot"/> with a flattened jellyroll topology <ref name="Volanakis"/> and a long <scene name='71/719862/Helix/1'>α-helix</scene> (residues 168-176) lies folded against the β-sheets. The predominant structure is β-sheet <ref>PMID: 1382589</ref> but short helical regions can be noticed for the residues 43 and 185 <ref name="kumar"/>. The carboxyl terminal end of the helix along with loop 177-182 form one of the two sides of a cleft that extends from the centre of the promoter to its edge at the central pore of the pentamer <ref name="Volanakis"/>. The other side of the cleft is formed by parts of the amino and carboxyl termini of the promoter <ref name="Volanakis"/>. This furrow is 24 Å long, 7.5 Å deep and 12.4 Å wide. The side walls are constructed from Ser5, Arg6, Gln203, Pro206, Trp187, Arg188, Asn160, Gly177, Leu176, Tyr175, His95 and Asp112 <ref name="Thompson"/>. This cleft is involved in C1q binding and perhaps also with the FcR binding <ref name="Volanakis"/>.<ref name="duclos">PMID: 15531769 </ref><ref name="Volanakis"/>.The outer part of the furrow is positively charged but the inner part terminates halfway through the pentamer pore at residue Asp112, providing a ring of negative charges lining the pore <ref name="Thompson"/>. Asp112 seems to be an important residue for recognition of Cq1 by CRP <ref name="Thompson"/> because it is considered, with Tyr175, to be C1q contact residues <ref name="Volanakis"/>. Glu88 seems to influence the conformational change of C1q necessary for complement activation, while Asn158 and His38 may contribute to the correct geometry of the binding site <ref name="Volanakis"/>.<br /> <br /> On the other face of the protomer (face A), two calcium ions are bound 4 Å apart by protein sidechains coming from loops collected at the concave face (face B) and this is the site of ligand binding <ref name="Thompson"/>. Each subunit in CRP is rotated by 22° towards the fivefold axis such that the helices of face A are 5 Å closer to the axis and the calcium sites on face B move away by an equivalent amount <ref name="Volanakis"/><ref name="Thompson"/>.<br /> Thus, CRP pentamer has two faces: a face that exibit the five phosphocholine binding sites and a face involve in the binding of C1q and possibly Fcr <ref name="Volanakis"/>.<br /> <br /> The five protomers are related one with an other by three salt bridges that mainly involve the 115-123 loop of one protomer and the 40-42 and 197-202 regions of the other promoter <ref name="Volanakis"/>.<br /> <br /> <br /> === Ca<sup>2+</sup>-binding site ===<br /> CRP is a calcium dependent structure. The face B binds two Ca<sup>2+</sup> ions per subunit. The ligands are bound asymmetrically in both Ca<sup>2+</sup>-binding sites. The residues of the site 1 include Asp60, Asn61, Glu138, Asp140, the carbonyl oxygen of the residue 139 and one oxygen of Asp60. The site 1 provides a total of five ligands for the Ca<sup>2+</sup> ion. The site 2 residues include Gln138, Asp140, Gln150 and non-coordinating Glu147. The site 2 provides four ligands for the Ca<sup>2+</sup> ion. The two Ca<sup>2+</sup>-binding sites are of equal affinity for Ca<sup>2+</sup> and are only differentiated by the carbonyl oxygen ligand. In presence of Ca<sup>2+</sup>, the two Ca<sup>2+</sup>-binding sites are overlapping in a loop. When the Ca<sup>2+</sup> sites are free, the residues 140 to 150 form a loop away from the molecule<ref name="Thompson"/>. This releases the proteolysis site <ref name="agrawal"/>, which induces the cleavage of CRP between Asn145 and Phe146 by nagarase protease and between Phe146 and Glu147 by pronase <ref name="ramadan">PMID: 12037301</ref>. Therefore Ca<sup>2+</sup> protects CRP form proteolytic cleavage and from degradation <ref name="agrawal"/>.<br /> <br /> === Phosphocholine-binding site ===<br /> PC stands for phosphocholine. It is a phospholipid in cell membranes and a plasma lipoprotein <ref name="Thompson"/>. The PC-binding site is a hydrophobic pocket constituted by the residues Leu64, Phe66, Thr76 and the two Ca<sup>2+</sup> <ref name="agrawal"/>.<br /> The choline function of PC interacts with the two key residues Phe66 and Glu81, therefore PC lies inside the PC-binding site <ref name="kumar"/> <ref name="agrawal"/>.<br /> The PC-binding site is next to the Ca<sup>2+</sup>-binding sites on the same face of the CRP protein. The phosphate groupe of PC interacts by coordination with the two Ca<sup>2+</sup> <ref name="agrawal"/>.<br /> The affinity of CRP for PC increases with the concentration of PC. A surface containing a high density of PC, such as C-polycaccharide, is therefore propitious to the CRP-binding <ref name="duclos"/>.<br /> CRP can also bind chromatin, histones, small nuclear ribonucleoproteins nuclear envelop proteins and nucleosomes Ca<sup>2+</sup>-dependently <ref name="agrawal"/>.<br /> [[Image:Phosphocholine.PNG | thumb | PC and Ca<sup>2+</sup>-binding site <ref>The PyMOL Molecular Graphics System, Version 1.8 Schrödinger, LLC.</ref>]]<br /> <br /> == Function ==<br /> CRP is involved in the primary and innate host defense. PC is present in teichoic acids, capsular carbohydrates, and lipopolysaccharides of bacteria and other micro-organisms. There are many PC-expressing micro-organisms such as ''Streptococcus pneumoniae'', ''Haemophilus influenzae'', ''Pseudomonas aeruginosa'', ''Neisseria meningitides'' and ''Neisseria gonorrhoeae'', ''Proteus morganii and Aspergillus fumigatus'' <ref name="Volanakis"/>. It binds to PC located on the surface of pathogens bacteria that infected the organism. The resulting immune response is the phagocytosis of PC-expressing bacteria <ref name="agrawal"/>. Moreover, apoptic and necrotic cells which belong to the host organism can be treated by the CRP resulting in a restoration of function in targeted tissues <ref name="Volanakis"/>. The CRP is therefore part of the acute phase response which is a rapid concentration variation of plasma proteins <ref name = "Alex">PMID: 12616974</ref>. <br /> When CRP is bind to a multivalent ligand, C1q is able to recognize it. This mechanism is initiated the C3 convertase assembly, which is an enzyme involved in the innate response. Furthermore, multiple pentamers have to be close to each other in order to realize this assembly <ref name="Volanakis"/>. <br /> <br /> == Biomedical interest ==<br /> Healthy humans have a CRP rate which is generally about 1 μg/mL<ref name="kumar"/>. CRP is secreted by the liver into the blood circulation<ref name = "Alex"/>. CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease<ref name="Thompson" />. CRP can be defined as a target for the development of cardioprotection and neuroprotection<ref name="kumar"/>.<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2525535 Sandbox Reserved 1121 2016-01-28T14:47:53Z

<p>Camille Mathieu: </p> <hr /> <div><Structure load='1B09' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <br /> Human C-Reactive Protein (CRP) is an acute phase protein belonging to the highly conserved pentraxin protein family, like as its homologue, the Serum Amyloid P component (SAP) <ref name="Thompson">PMID: 10368284</ref>. Although it is a normal serum protein, its circulating concentration raises rapidly and extensively in a cytokine-mediated in response to an infection, an inflammation or a tissue injury. In this way, serum CRP rate is empirically dose to detect many human disease <ref name="Thompson"/>. CRP was named this way because it was found that the protein could precipitate the "C" polysaccharide derived from Streptococcus pneumoniae cell wall <ref>PMID: 15337754</ref><ref name="kumar">PMID: 21541851</ref>.<br /> <br /> <br /> <br /> == Structure ==<br /> === CRP structure ===<br /> <br /> The crystal structure of CRP was determined by using SAP as the search model <ref name="Thompson"/>. The structure of CRP has been determined by X-ray crystallography at 3 Å resolution. Like SAP, the protein consists of five protomers, uncovalently bonded and nonglycosylated that are arranged symmetrically around a central pore <ref name="Volanakis">PMID: 11532280</ref>. Each subunit is a 25 kDa protein consisting of 224 residues <ref name="uniprot">[http://www.uniprot.org/uniprot/P02741 UniProtKB - P02741 (CRP_HUMAN)]</ref>. The diameter of the CRP pentamer is 102 Å, the inner pore diameter is 30 Å and the diameter of a subunit is 36 Å <ref name="agrawal">PMID: 19799114 </ref><ref name="Volanakis"/>.Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP <ref name="kumar"/>.<br /> <br /> Each subunit consist of two antiparallel <scene name='71/719862/Sheet/1'>β-sheets</scene> <ref name="uniprot"/> with a flattened jellyroll topology <ref name="Volanakis"/> and a long <scene name='71/719862/Helix/1'>α-helix</scene> (residues 168-176) lies folded against the β-sheets <ref name="Volanakis"/>. The predominant structure is β-sheet <ref>PMID: 1382589</ref> but short helical regions can be noticed for the residues 43 and 185 <ref name="kumar"/>. <br /> <br /> In each subunit, we can distinguish 2 faces: A and B. Two calcium ions are bound 4 Å apart by protein sidechains coming from loops collected at the concave face (B) and this is the site of ligand binding <ref name="Thompson"/>. The A face is recognizable by the presence of a single α-helix, meaning that this face of the pentamer shows five helices. There is also a marked furrow of 24 Å long, 7.5 Å deep and 12.4 Å wide. The side walls are constructed from Ser5, Arg6, Gln203, Pro206, Trp187, Arg188, Asn160, Gly177, Leu176, Tyr175, His95 and Asp112 <ref name="Thompson"/>. The outer part of the furrow is positively charged but the inner part terminates halfway through the pentamer pore at residue Asp112, providing a ring of negative charges lining the pore <ref name="Thompson"/>. This face can interact with C1q and Fc receptors <ref name="duclos">PMID: 15531769 </ref><ref name="Volanakis"/>. Asp112 seems to be an important residue for recognition of Cq1 by CRP <ref name="Thompson"/>. Each subunit in CRP is rotated by 22° towards the fivefold axis such that the helices of face A are 5 Å closer to the axis and the calcium sites on face B move away by an equivalent amount. <br /> <br /> === Ca<sup>2+</sup>-binding site ===<br /> CRP is a calcium dependent structure. The face B binds two Ca<sup>2+</sup> ions per subunit. The ligands are bound asymmetrically in both Ca<sup>2+</sup>-binding sites. The residues of the site 1 include Asp60, Asn61, Glu138, Asp140, the carbonyl oxygen of the residue 139 and one oxygen of Asp60. The site 1 provides a total of five ligands for the Ca<sup>2+</sup> ion. The site 2 residues include Gln138, Asp140, Gln150 and non-coordinating Glu147. The site 2 provides four ligands for the Ca<sup>2+</sup> ion. The two Ca<sup>2+</sup>-binding sites are of equal affinity for Ca<sup>2+</sup> and are only differentiated by the carbonyl oxygen ligand. When the Ca<sup>2+</sup> sites are free, the residues 140 to 150 form a loop away from the molecule<ref name="Thompson"/>. The two Ca<sup>2+</sup>-binding sites are overlapping in a loop. In the absence of Ca<sup>2+</sup>, the loop changes conformation and releases the proteolysis site <ref name="agrawal"/>, which induces the cleavage of CRP between Asn145 and Phe146 by nagarase protease and between Phe146 and Glu147 by pronase <ref name="ramadan">PMID: 12037301</ref>. Therefore Ca<sup>2+</sup> protects CRP form proteolytic cleavage and from degradation <ref name="agrawal"/>.<br /> <br /> === Phosphocholine-binding site ===<br /> PC stands for phosphocholine. It is a phospholipid in cell membranes and a plasma lipoprotein <ref name="Thompson"/>. The PC-binding site is a hydrophobic pocket constituted by the residues Leu64, Phe66, Thr76 and the two Ca<sup>2+</sup> <ref name="agrawal"/>.<br /> The choline function of PC interacts with the two key residues Phe66 and Glu81, therefore PC lies inside the PC-binding site <ref name="kumar"/> <ref name="agrawal"/>.<br /> The PC-binding site is next to the Ca<sup>2+</sup>-binding sites on the same face of the CRP protein. The phosphate groupe of PC interacts by coordination with the two Ca<sup>2+</sup> <ref name="agrawal"/>.<br /> The affinity of CRP for PC increases with the concentration of PC. A surface containing a high density of PC, such as C-polycaccharide, is therefore propitious to the CRP-binding <ref name="duclos"/>.<br /> CRP can also bind chromatin, histones, small nuclear ribonucleoproteins nuclear envelop proteins and nucleosomes Ca<sup>2+</sup>-dependently <ref name="agrawal"/>.<br /> [[Image:Phosphocholine.PNG | thumb | PC and Ca<sup>2+</sup>-binding site <ref>The PyMOL Molecular Graphics System, Version 1.8 Schrödinger, LLC.</ref>]]<br /> <br /> == Function ==<br /> CRP is involved in the primary and innate host defense <ref name="Volanakis"/>. It binds to PC located on the surface of pathogens bacteria that infected the organism. The resulting immune response is the phagocytosis of PC-expressing bacteria <ref name="agrawal"/>. Moreover, apoptic and necrotic cells which belong to the host organism can be treated by the CRP resulting in a restoration of function in targeted tissues <ref name="Volanakis"/>. The CRP is therefore part of the acute phase response which is a rapid concentration variation of plasma proteins <ref name = "Alex">PMID: 12616974</ref>. <br /> When CRP is bind to a multivalent ligand, C1q is able to recognize it. This mechanism is initiated the C3 convertase assembly, which is an enzyme involved in the innate response. Furthermore,multiple pentamers have to be close to each other in order to realize this assembly <ref name="Volanakis"/>. <br /> <br /> == Biomedical interest ==<br /> Healthy humans have a CRP rate which is generally about 1 μg/mL<ref name="kumar"/>. CRP is secreted by the liver into the blood circulation<ref name = "Alex"/>. CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease<ref name="Thompson" />. CRP can be defined as a target for the development of cardioprotection and neuroprotection<ref name="kumar"/>.<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523127 Sandbox Reserved 1121 2016-01-26T21:15:15Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Ca<sup>2+</sup> binding-site ===<br /> CRP is a calcium dependent structure. Effectively, Ca<sup>2+</sup> is required for PC binding, and more precisely for the formation of the PC binding site thanks to structural rearrangements. The protection against denaturation and proteolysis is performed through Ca<sup>2+</sup> binding too. In the absence of Ca<sup>2+</sup>, hCRP is cleaved between Asn145 and Phe146 by nagarse protease, and between Phe146 and Glu147 by pronase. <br /> Asp60, Asn61, Glu138, Asp140 and the main-chain carbonyl of Gln139 residues allow the first calcium ion binding, and the second is performed through Glu138, Asp140, Glu147 and Gln150.<ref name="ramadan">Ramadan, M. A. M., Shrive, A. K., Holden, D., Myles, D. A. A., Volanakis, J. E., Larry J.DeLucas, L. J., Greenhough, T. J. (2002), The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals, Acta Cryst., D58 :992-1001</ref><br /> <br /> === PC binding site ===<br /> PC stands for phosphocholine. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> Healthy humans have CRP rate which is generally about 1 μg/mL.<ref name="kumar"/> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /> CRP can be defined as a target for the development of cardioprotection and neuroprotection.<ref name="kumar"/><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523126 Sandbox Reserved 1121 2016-01-26T21:13:30Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> CRP is a calcium dependent structure. Effectively, Ca<sup>2+</sup> is required for PC binding, and more precisely for the formation of the PC binding site thanks to structural rearrangements. The protection against denaturation and proteolysis is performed through Ca2+ binding too. In the absence of Ca2+, hCRP is cleaved between Asn145 and Phe146 by nagarse protease, and between Phe146 and Glu147 by pronase. <br /> Asp60, Asn61, Glu138, Asp140 and the main-chain carbonyl of Gln139 residues allow the first calcium ion binding, and the second is performed through Glu138, Asp140, Glu147 and Gln150.<ref name="ramadan">Ramadan, M. A. M., Shrive, A. K., Holden, D., Myles, D. A. A., Volanakis, J. E., Larry J.DeLucas, L. J., Greenhough, T. J. (2002), The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals, Acta Cryst., D58 :992-1001</ref><br /> <br /> === PC binding site ===<br /> PC stands for phosphocholine. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> Healthy humans have CRP rate which is generally about 1 μg/mL.<ref name="kumar"/> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /> CRP can be defined as a target for the development of cardioprotection and neuroprotection.<ref name="kumar"/><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523124 Sandbox Reserved 1121 2016-01-26T21:06:44Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> CRP is a calcium dependent structure. Effectively, Ca2+ is required for PC binding, and more precisely for the formation of the PC binding site thanks to structural rearrangements. The protection against denaturation and proteolysis is performed through Ca2+ binding too. In the absence of Ca2+, hCRP is cleaved between Asn145 and Phe146 by nagarse protease, and between Phe146 and Glu147 by pronase. <br /> Asp60, Asn61, Glu138, Asp140 and the main-chain carbonyl of Gln139 residues allow the first calcium ion binding, and the second is performed through Glu138, Asp140, Glu147 and Gln150.<ref name="ramadan">Ramadan, M. A. M., Shrive, A. K., Holden, D., Myles, D. A. A., Volanakis, J. E., Larry J.DeLucas, L. J., Greenhough, T. J. (2002), The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals, Acta Cryst., D58 :992-1001</ref><br /> <br /> === PC binding site ===<br /> PC stands for phosphocholine. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> Healthy humans have CRP rate which is generally about 1 μg/mL.<ref name="kumar"/> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /> CRP can be defined as a target for the development of cardioprotection and neuroprotection.<ref name="kumar"/><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523119 Sandbox Reserved 1121 2016-01-26T20:58:30Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> CRP is a calcium dependent structure. Effectively, Ca2+ is required for PC binding, and more precisely for the formation of the PC binding site thanks to structural rearrangements. The protection against denaturation and proteolysis is performed through Ca2+ binding too. In the absence of Ca2+, hCRP is cleaved between Asn145 and Phe146 by nagarse protease, and between Phe146 and Glu147 by pronase. <ref name="ramadan">Ramadan, M. A. M., Shrive, A. K., Holden, D., Myles, D. A. A., Volanakis, J. E., Larry J.DeLucas, L. J., Greenhough, T. J. (2002), The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals, Acta Cryst., D58 :992-1001</ref><br /> <br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> Healthy humans have CRP rate which is generally about 1 μg/mL.<ref name="kumar"/> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /> CRP can be defined as a target for the development of cardioprotection and neuroprotection.<ref name="kumar"/><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523115 Sandbox Reserved 1121 2016-01-26T20:56:10Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> CRP is a calcium dependent strcuture. Effectively, Ca2+ is required for PC binding, and more precisely for the formation of the PC binding site. Structural rearrangements of the CRP occur when the protein binds Ca2+. The protection against denaturation and proteolysis is performed through Ca2+ binding too. In the absence of Ca2+, hCRP is cleaved between Asn145 and Phe146 by nagarse protease, and between Phe146 and Glu147 by pronase. <ref name="ramadan">Ramadan, M. A. M., Shrive, A. K., Holden, D., Myles, D. A. A., Volanakis, J. E., Larry J.DeLucas, L. J., Greenhough, T. J. (2002), The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals, Acta Cryst., D58 :992-1001</ref><br /> <br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> Healthy humans have CRP rate which is generally about 1 μg/mL.<ref name="kumar"/> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /> CRP can be defined as a target for the development of cardioprotection and neuroprotection.<ref name="kumar"/><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523112 Sandbox Reserved 1121 2016-01-26T20:50:36Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> CRP is a calcium dependent strcuture. Effectively, Ca2+ is required for PC binding, and more precisely for the formation of the PCbinding site. Structural rearrangements of the CRP occur when the protein binds calcium. The protection against denaturation and proteolysis. <ref name="ramadan">Ramadan, M. A. M., Shrive, A. K., Holden, D., Myles, D. A. A., Volanakis, J. E., Larry J.DeLucas, L. J., Greenhough, T. J. (2002), The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals, Acta Cryst., D58 :992-1001</ref><br /> <br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> Healthy humans have CRP rate which is generally about 1 μg/mL.<ref name="kumar"/> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /> CRP can be defined as a target for the development of cardioprotection and neuroprotection.<ref name="kumar"/><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523103 Sandbox Reserved 1121 2016-01-26T20:33:19Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar"/><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> Healthy humans have CRP rate which is generally about 1 μg/mL.<ref name="kumar"/> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /> CRP can be defined as a target for the development of cardioprotection and neuroprotection.<ref name="kumar"/><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523099 Sandbox Reserved 1121 2016-01-26T20:29:55Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar"/><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> Healthy humans have CRP rate which is generally about 1 μg/mL.<ref name="kumar"/> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523092 Sandbox Reserved 1121 2016-01-26T20:25:25Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar"/><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet <ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523089 Sandbox Reserved 1121 2016-01-26T20:22:16Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar"/><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523088 Sandbox Reserved 1121 2016-01-26T20:19:22Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar"/><br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523086 Sandbox Reserved 1121 2016-01-26T20:16:05Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> === CRP structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/><br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523084 Sandbox Reserved 1121 2016-01-26T20:13:22Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> === Primary structure ===<br /> Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequenceof CRP.<ref name="kumar"/> <br /> ===Secondary structure and more===<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> === PC binding site ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523080 Sandbox Reserved 1121 2016-01-26T20:07:06Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <ref name="kumar">Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505</ref><br /> === PC interaction ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523076 Sandbox Reserved 1121 2016-01-26T20:00:59Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /><br /> === Calcium binding-site ===<br /> <br /> === PC interaction ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523075 Sandbox Reserved 1121 2016-01-26T19:58:46Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded). <ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref><br /> === Calcium binding-site ===<br /> <br /> === PC interaction ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thompson" /><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523074 Sandbox Reserved 1121 2016-01-26T19:57:28Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded). <ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref><br /> === Calcium binding-site ===<br /> <br /> === PC interaction ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thomspon">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref name="thomspon"></ref><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523073 Sandbox Reserved 1121 2016-01-26T19:55:24Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded). <ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref><br /> === Calcium binding-site ===<br /> <br /> === PC interaction ===<br /> PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref>Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<ref>Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref><br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523072 Sandbox Reserved 1121 2016-01-26T19:52:47Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded). <ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref><br /> === Calcium binding-site ===<br /> <br /> === PC interaction ===<br /> <br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<br /> <ref>Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.<br /> Moreover<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523071 Sandbox Reserved 1121 2016-01-26T19:49:09Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded). <ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref><br /> === Calcium binding-site ===<br /> <br /> === PC interaction ===<br /> <br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.<br /> <ref>http://biomednet.com/elecref/0969212600700169<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2523069 Sandbox Reserved 1121 2016-01-26T19:44:36Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> == Human C-reactive protein complexed with phosphocholine ==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded). <ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref><br /> === Calcium binding-site ===<br /> <br /> === PC interaction ===<br /> <br /> <br /> == Function ==<br /> <br /> == Biomedical interest ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=Sandbox_Reserved_1121&diff=2522904 Sandbox Reserved 1121 2016-01-25T12:34:25Z

<p>Camille Mathieu: </p> <hr /> <div>{{Sandbox_Reserved_ESBS_2015}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Structure ==<br /> <br /> == Disease ==<br /> therapeutical<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Camille Mathieu https://proteopedia.org/index.php?title=User:Camille_Mathieu&diff=2522635 User:Camille Mathieu 2016-01-21T18:05:19Z

<p>Camille Mathieu: </p> <hr /> <div>* Full Real Name:Camille MATHIEU<br /> <br /> * Position:Student<br /> <br /> * Institution (NO ABBREVIATIONS):Ecole Superieure de Biotechnologies de Strasbourg<br /> <br /> * City, State/Province, Country:Strasbourg, France<br /> <br /> * Field of Expertise or Study:biotechnology</div>

Camille Mathieu