Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Apr 12;13:1955. doi: 10.1038/s41467-022-29580-2

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 9 — a Schematic representation of CR3 (extended closed conformation), C3dg, and iC3b (upright conformation). Domains and salient features are labeled. b Model of the iC3b–CR3 interaction across the gap between a macrophage (brown band, top) and a heterogeneous iC3b- and C3dg-opsonized surface (grey surface, bottom). iC3b and C3dg are covalently attached to the opsonized surface via a covalent bond involving the Gln991 carbonyl ester (orange star). Two types of iC3b–CR3 (extended open conformation) complexes are depicted: a hybrid complex whereby the TED domain and the C3c subunit in contact with the same CR3 come from different but adjacent iC3b molecules; and a binary heterocomplex involving a single iC3b molecule. The short intracellular region of CR3 is shown interacting with talin and kindlin in some complexes, which in turn recruit the force-producing actomyosin cytoskeleton responsible for the pulling forces necessary for phagocytosis.