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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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,...
Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Related Experiment Video

Updated: Jun 21, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Multimeric and trimeric subunit SP-D are interconvertible structures with distinct ligand interaction.

Grith L Sorensen1, Silje V Hoegh, Rikke Leth-Larsen

  • 1Medical Biotechnology Center, University of Southern Denmark, DK-5000 Odense C, Denmark. glsorensen@health.sdu.dk

Molecular Immunology
|July 7, 2009
PubMed
Summary
This summary is machine-generated.

Surfactant protein-D (SP-D) exists as trimers and multimers. These forms have distinct binding properties to microbes and lipoproteins, indicating separate roles in innate immunity.

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Related Experiment Videos

Last Updated: Jun 21, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Area of Science:

  • Immunology
  • Biochemistry
  • Structural Biology

Background:

  • Surfactant protein-D (SP-D) is a key innate immune lectin involved in microbial clearance.
  • SP-D exists in trimeric and multimeric forms, influenced by N-terminal structure and glycosylation.
  • Multimerization is crucial for enhancing SP-D's microbial phagocytosis capabilities.

Purpose of the Study:

  • To isolate and characterize distinct trimeric and multimeric forms of human SP-D.
  • To investigate the interconversion and biochemical properties of these SP-D structural forms.
  • To determine the differential binding affinities of trimeric and multimeric SP-D to microbial components and lipoproteins.

Main Methods:

  • Isolation of defined multimeric SP-D forms from human amniotic fluid.
  • Utilized ManNAc-affinity chromatography for SP-D subunit and multimer purification.
  • Employed solid-phase assays to assess binding interactions of different SP-D forms.

Main Results:

  • Affinity chromatography yielded both trimeric SP-D subunits and multimers, with some interconversion observed.
  • The distribution of SP-D forms was independent of the Met11Thr genotype.
  • Trimeric SP-D exhibited stronger binding to LPS, PGN, LDL, oxLDL, and HDL, but weaker binding to mannan and LTA compared to multimers.

Conclusions:

  • Purified trimeric and multimeric SP-D represent distinct molecular populations.
  • These forms exhibit differential binding profiles, suggesting specialized functions in innate immunity.
  • SP-D structural forms are partly interconvertible, with unique disulfide crosslinking patterns.