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Related Concept Videos

Complement System01:27

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
CRISPR and crRNAs02:53

CRISPR and crRNAs

Bacteria and archaea are susceptible to viral infections just like eukaryotes; therefore, they have developed a unique adaptive immune system to protect themselves. Clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins (CRISPR-Cas) are present in more than 45% of known bacteria and 90% of known archaea.
The CRISPR-Cas system stores a copy of foreign DNA in the host genome and uses it to identify the foreign DNA upon reinfection. CRISPR-Cas has three different...

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Related Experiment Video

Updated: May 30, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

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Structures of the rat complement regulator CrrY.

Pietro Roversi1, Steven Johnson, Joseph J E Caesar

  • 1Sir William Dunn School of Pathology, Oxford University, South Parks Road, Oxford OX4 3RE, England.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
|July 29, 2011
PubMed
Summary
This summary is machine-generated.

Complement receptor 1-related protein Y (CrrY), a rodent-specific complement regulator, has a unique bend between domains 3 and 4. This structural feature may facilitate its interaction with C3b during complement regulation.

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High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry
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Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry

Published on: May 19, 2020

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Complement receptor 1-related protein Y (CrrY) is a cell-surface protein regulating the complement system.
  • CrrY is unique to rodent species, making it a valuable model for studying complement regulation.

Purpose of the Study:

  • To determine the three-dimensional structure of rat CrrY domains 1-4.
  • To investigate the structural basis for CrrY's function as a complement regulator.

Main Methods:

  • X-ray crystallography was used to determine the structure of rat CrrY domains 1-4 in two distinct crystal forms.
  • Structural comparisons were made with other known complement regulators.

Main Results:

  • The crystal structures revealed a significant 70° bend between domains 3 and 4 of CrrY.
  • This unique structural conformation was observed in both determined crystal forms.

Conclusions:

  • The identified bend between domains 3 and 4 of CrrY is a key structural feature.
  • This structural flexibility may be crucial for CrrY's interaction and complex formation with C3b, suggesting a mechanism for complement regulation.