Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones

Catterall, Catherine; Lyons, A. Bruce; Sim, R. B.; Day, Anthony J.; Harris, Tim

doi:10.1042/bj2420849

Cited by 114 publications

(68 citation statements)

References 39 publications

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“…Previous studies suggest the occurrence of a disulfide bridge between Cys 8° and Cys 91 [31,32]. As analysis of E18, CB 1, and SK2 showed, we were able to prepare samples from various digests that essentially contained both N-terminal domains.…”

Section: Discussionmentioning

confidence: 81%

Identification of disulfide bonds in the ninth component (C9) of human complement

1996

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Section: Discussionmentioning

confidence: 81%

Identification of disulfide bonds in the ninth component (C9) of human complement

1996

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“…To clarify the mutation in patient B, we cloned the PCR product spanning exon 7 using the pGEMTeasy Cloning Kit (Promega, Madison, WI) and sequenced it as above. Nucleotide and amino acid numbering was according to the published cDNA sequence (accession number M25615) (19). Nucleotide 1 is located 29 nucleotides before the start of the peptide signal sequence.…”

Section: Dna Analysismentioning

confidence: 99%

Mutations in Complement Factor I Predispose to Development of Atypical Hemolytic Uremic Syndrome

Kavanagh¹,

Kemp²,

Mayland³

et al. 2005

Journal of the American Society of Nephrology

314

168

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Mutations in the plasma complement regulator factor H (CFH) and the transmembrane complement regulator membrane co-factor protein (MCP) have been shown to predispose to atypical hemolytic uremic syndrome (HUS). Both of these proteins act as co-factors for complement factor I (IF). IF is a highly specific serine protease that cleaves the ␣-chains of C3b and C4b and thus downregulates activation of both the classical and the alternative complement pathways. This study looked for IF mutations in a panel of 76 patients with HUS. Mutations were detected in two patients, both of whom had reduced serum IF levels. A heterozygous bp change, c.463 G>A, which results in a premature stop codon (W127X), was found in one, and in the other, a heterozygous single base pair deletion in exon 7 (del 922C) was detected. Both patients had a history of recurrent HUS after transplantation. This is in accordance with the high rate of recurrence in patients with CFH mutations. Patients who are reported to have mutations in MCP, by contrast, do not have recurrence after transplantation. As with CFH-and MCPassociated HUS, there was incomplete penetrance in the family of one of the affected individuals. This study provides further evidence that atypical HUS is a disease of complement dysregulation.

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“…The LDLr2 coding sequence of factor I (residues 240-276 [3]) was amplified from a cDNA clone [3] by PCR at an annealing temperature of 42°C with the following primers: 5' oligonucleotide GCA TGC CAA GGC AAA GGC TTC, 3' oligonucleotide CGG ATC CTA TGC ACA GCC AAC TTC ATC TTC. The underlined region in the 3' oligonucleotide corresponds to a BamHI restriction site used to identify positive clones and the region shown in bold corresponds to a translation termination codon.…”

mentioning

confidence: 99%

β‐Sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy

et al. 1995

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Low density lipoprotein receptor domains (LDLrs) represent a large cell surface receptor superfamily of consensus length 39 residues. Alignment of 194 sequences indicated highly conserved Cys and Asp/Glu residues, and a consensus secondary structure with three fl-strands was predicted. Sequence threading against known protein folds indicated consistency with small flsheet proteins. Complement factor I contains two LDLrs, and the second of these was successfully expressed using a bacterial pGEX system. FT-IR spectroscopy on this indicated a small amount of fl-sheet together with turns and loops. LDLr is proposed to have a fl-sheet structure in which the five biologically important Asp/Glu residues are located on an exposed loop.Key words: LDLr domain; FT-IR spectroscopy; Secondary structure prediction; Protein fold recognition; fl-Sheet protein basic amino acids in other ligands [2]. LDLr-3 to LDLr-7 in the LDL receptor are essential for apoprotein B binding, and LDLr-5 is essential for apoprotein E binding. In the ~2M receptor, a fragment with eight LDLr domains binds to ~2 M.A powerful strategy to analyse protein structures has been developed, based on the joint use of (a) averaged secondary structure predictions to define structural elements, (b) sequence threading against known protein folds to identify related protein folds, and (c) spectroscopy to identify the secondary structure [6,7]. By this approach, we show that LDLr contains turns and loops with a small amount of fl-strand, and propose that the biologically important Asp/Glu residues are located on a surface loop.

show abstract

Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones

Cited by 114 publications

References 39 publications

Identification of disulfide bonds in the ninth component (C9) of human complement

Identification of disulfide bonds in the ninth component (C9) of human complement

Mutations in Complement Factor I Predispose to Development of Atypical Hemolytic Uremic Syndrome

β‐Sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy

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