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{{Theoretical_model}} | |||
==HOMOLOGY MODEL OF HUMAN FACTOR H SCRS 6 AND 7== | |||
<StructureSection load='1kov' size='340' side='right'caption='[[1kov]]' 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=1KOV 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=1kov FirstGlance], [https://www.ebi.ac.uk/pdbsum/1kov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kov ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Factor H, a secretory glycoprotein comprising 20 short consensus repeat (SCR) or 'sushi' domains of about 60 amino acids each, is a regulator of the complement system. The complement-regulatory functions of factor H are targeted by its binding to polyanions such as heparin/sialic acid, involving SCRs 7 and 20. Recently, the SCR 7 heparin-binding site was shown to be co-localized with the Streptococcus Group A M protein binding site on factor H (T.K. Blackmore et al., Infect. Immun. 66, 1427 (1998)). Using sequence analysis of all heparin-binding domains of factor H and its closest homologues, molecular modeling of SCRs 6 and 7, and surface electrostatic potential studies, the residues implicated in heparin/sialic acid binding to SCR 7 have been localized to four regions of sequence space containing stretches of basic as well as histidine residues. The heparin-binding site is spatially compact and lies near the interface between SCRs 6 and 7, with residues in the interdomain linker playing a significant role. | |||
Pinpointing the putative heparin/sialic acid-binding residues in the 'sushi' domain 7 of factor H: a molecular modeling study.,Ranganathan S, Male DA, Ormsby RJ, Giannakis E, Gordon DL Pac Symp Biocomput. 2000;:155-67. PMID:10902165<ref>PMID:10902165</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1kov" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Giannakis, E]] | |||
[[Category: Gordon, D L]] | |||
[[Category: Male, D A]] | |||
[[Category: Ormsby, R J]] | |||
[[Category: Ranganathan, S]] | |||
Latest revision as of 09:33, 18 August 2021
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HOMOLOGY MODEL OF HUMAN FACTOR H SCRS 6 AND 7HOMOLOGY MODEL OF HUMAN FACTOR H SCRS 6 AND 7
Structural highlights
Publication Abstract from PubMedFactor H, a secretory glycoprotein comprising 20 short consensus repeat (SCR) or 'sushi' domains of about 60 amino acids each, is a regulator of the complement system. The complement-regulatory functions of factor H are targeted by its binding to polyanions such as heparin/sialic acid, involving SCRs 7 and 20. Recently, the SCR 7 heparin-binding site was shown to be co-localized with the Streptococcus Group A M protein binding site on factor H (T.K. Blackmore et al., Infect. Immun. 66, 1427 (1998)). Using sequence analysis of all heparin-binding domains of factor H and its closest homologues, molecular modeling of SCRs 6 and 7, and surface electrostatic potential studies, the residues implicated in heparin/sialic acid binding to SCR 7 have been localized to four regions of sequence space containing stretches of basic as well as histidine residues. The heparin-binding site is spatially compact and lies near the interface between SCRs 6 and 7, with residues in the interdomain linker playing a significant role. Pinpointing the putative heparin/sialic acid-binding residues in the 'sushi' domain 7 of factor H: a molecular modeling study.,Ranganathan S, Male DA, Ormsby RJ, Giannakis E, Gordon DL Pac Symp Biocomput. 2000;:155-67. PMID:10902165[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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