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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1998-4-21
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pubmed:abstractText |
Complement factor H (fH) regulates activation of the alternative pathway of C, reducing the amount of C3b deposited on sialic acid-rich surfaces. Heparin binding has been used as a model for examining the sialic acid-binding characteristics of fH. We have previously shown that of the 20 short consensus repeat (SCR) modules of fH, SCR 7 contains an important heparin binding site, but other SCRs also play a role in heparin binding. To localize the other sites, we prepared recombinant truncated and SCR deletion mutants of fH and tested them by heparin-agarose affinity chromatography. The 5 C-terminal SCRs were found to contain a heparin binding site as an SCR 7 deletion mutant of the N terminal 15 SCRs did not bind heparin, but a construct consisting of SCRs 16-20 was shown to bind heparin. Double deletion of SCRs 7 and 20 from fH abrogated binding to heparin, indicating that SCR 20 contains a heparin binding site. This finding was confirmed with the observation that attachment of SCR 20 to a group of nonbinding SCRs produced a heparin-binding protein. A protein consisting of SCRs 19 and 20 did not bind heparin, whereas SCRs 18-20 did, indicating that, although SCR 20 contains a heparin binding site, at least two nonspecific adjacent SCRs are required. fH-related protein-3 (FHR-3) possesses an SCR homologous to SCR 7 of fH and bound heparin, whereas FHR-4, which lacks such an SCR, did not. Thus, fH contains two separate heparin binding sites, which are located in SCRs 7 and 20.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CFHR3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CFHR4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Factor H,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/complement factor H, human
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
160
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3342-8
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pubmed:dateRevised |
2010-5-20
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pubmed:meshHeading |
pubmed-meshheading:9531293-Apolipoproteins,
pubmed-meshheading:9531293-Binding Sites,
pubmed-meshheading:9531293-Blood Proteins,
pubmed-meshheading:9531293-Complement Factor H,
pubmed-meshheading:9531293-Consensus Sequence,
pubmed-meshheading:9531293-Heparin,
pubmed-meshheading:9531293-Humans,
pubmed-meshheading:9531293-Protein Structure, Tertiary,
pubmed-meshheading:9531293-Recombinant Proteins,
pubmed-meshheading:9531293-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:9531293-Sequence Deletion
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pubmed:year |
1998
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pubmed:articleTitle |
Identification of the second heparin-binding domain in human complement factor H.
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pubmed:affiliation |
Department of Microbiology and Infectious Diseases, Flinders Medical Centre, Bedford Park, South Australia. tim.blackmore@flinders.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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