Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Crystallographic determination of the disease-associated T1184R variant of complement regulator factor H.

Acta crystallographica. Section D, Biological crystallography - 1 Jul 2011

Morgan Hugh P, Jiang Jingzi, Herbert Andrew P, Kavanagh David, Uhrin Dušan, Barlow Paul N, Hannan Jonathan P

Abstract excerpt

The soluble 155 kDa glycoprotein factor H (FH) protects host tissue from damage by the human complement system. It accelerates decay of the alternative-pathway C3 convertase, C3bBb, and is a cofactor for factor I-mediated cleavage of the opsonin C3b. Numerous mutations and single-nucleotide polymorphisms (SNPs) occur in the gene encoding FH and the resulting missense mutations and truncation products result in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Atypical Hemolytic Uremic Syndrome
Share to Complement Factor H

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Hemolytic-Uremic Syndrome

Share to Models, Molecular

Share to Mutation

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 21697597
DOI: 10.1107/S0907444911015423

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystallographic determination of the disease-associated T1184R variant of complement regulator factor H.PMID 21697597Read ↗

Structural Analysis of the C-Terminal Region (Modules 18–20) of Complement Regulator Factor H (FH)Semantic proximity Read ↗

Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.Semantic proximity Read ↗

Structural and functional characterization of the product of disease-related factor H gene conversion.Semantic proximity Read ↗

An interactive web database of factor H-associated hemolytic uremic syndrome mutations: insights into the structural consequences of disease-associated mutations.Semantic proximity Read ↗

The interactive Factor H-atypical hemolytic uremic syndrome mutation database and website: update and integration of membrane cofactor protein and Factor I mutations with structural models.Semantic proximity Read ↗

Translational mini-review series on complement factor H: structural and functional correlations for factor H.Semantic proximity Read ↗

New functional and structural insights from updated mutational databases for complement factor H, Factor I, membrane cofactor protein and C3Semantic proximity Read ↗

Antibody recognition of complement factor H reveals a flexible loop involved in atypical hemolytic uremic syndrome pathogenesis.Semantic proximity Read ↗

Both domain 19 and domain 20 of factor H are involved in binding to complement C3b and C3d.Semantic proximity Read ↗

Factor H and atypical hemolytic uremic syndrome: mutations in the C-terminus cause structural changes and defective recognition functions.Semantic proximity Read ↗

Factor H family proteins: on complement, microbes and human diseases.Semantic proximity Read ↗

A synthetic protein as efficient multitarget regulator against complement over-activationSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.