1lim: Difference between revisions
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[[ | ==COMPARATIVE ANALYSES OF PENTRAXINS: IMPLICATIONS FOR PROTOMER ASSEMBLY AND LIGAND BINDING== | ||
<StructureSection load='1lim' size='340' side='right'caption='[[1lim]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LIM FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lim FirstGlance], [https://www.ebi.ac.uk/pdbsum/1lim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lim ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BACKGROUND: Pentraxins are a family of plasma proteins characterized by their pentameric assembly and calcium-dependent ligand binding. The recent determination of the crystal structure for a member of this family, human serum amyloid P component (SAP), provides a basis for the comparative analysis of the pentraxin family. RESULTS: We have compared the sequences, tertiary structures and quaternary arrangements of SAP with human C-reactive protein (CRP), Syrian hamster SAP (HSAP) and Limulus polyphemus CRP (LIM). These proteins can adopt a beta-jelly roll topology and a hydrophobic core similar to that seen in SAP. Only minor differences are observed in the positions of residues involved in coordinating calcium ions. CONCLUSIONS: Calcium-mediated ligand binding by CRP, HSAP and LIM is similar to that defined by the crystal structure of SAP, but sequence differences in the hydrophobic pocket explain the differential ligand specificities exhibited by the homologous proteins. Differences elsewhere, including insertions and deletions, account for the different (hexameric) quaternary structure of LIM. | |||
Comparative analyses of pentraxins: implications for protomer assembly and ligand binding.,Srinivasan N, White HE, Emsley J, Wood SP, Pepys MB, Blundell TL Structure. 1994 Nov 15;2(11):1017-27. PMID:7881902<ref>PMID:7881902</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1lim" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Blundell, T L]] | [[Category: Blundell, T L]] | ||
[[Category: Emsley, J]] | [[Category: Emsley, J]] | ||
Latest revision as of 09:45, 18 August 2021
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COMPARATIVE ANALYSES OF PENTRAXINS: IMPLICATIONS FOR PROTOMER ASSEMBLY AND LIGAND BINDINGCOMPARATIVE ANALYSES OF PENTRAXINS: IMPLICATIONS FOR PROTOMER ASSEMBLY AND LIGAND BINDING
Structural highlights
Publication Abstract from PubMedBACKGROUND: Pentraxins are a family of plasma proteins characterized by their pentameric assembly and calcium-dependent ligand binding. The recent determination of the crystal structure for a member of this family, human serum amyloid P component (SAP), provides a basis for the comparative analysis of the pentraxin family. RESULTS: We have compared the sequences, tertiary structures and quaternary arrangements of SAP with human C-reactive protein (CRP), Syrian hamster SAP (HSAP) and Limulus polyphemus CRP (LIM). These proteins can adopt a beta-jelly roll topology and a hydrophobic core similar to that seen in SAP. Only minor differences are observed in the positions of residues involved in coordinating calcium ions. CONCLUSIONS: Calcium-mediated ligand binding by CRP, HSAP and LIM is similar to that defined by the crystal structure of SAP, but sequence differences in the hydrophobic pocket explain the differential ligand specificities exhibited by the homologous proteins. Differences elsewhere, including insertions and deletions, account for the different (hexameric) quaternary structure of LIM. Comparative analyses of pentraxins: implications for protomer assembly and ligand binding.,Srinivasan N, White HE, Emsley J, Wood SP, Pepys MB, Blundell TL Structure. 1994 Nov 15;2(11):1017-27. PMID:7881902[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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