1GKN

Structure Determination and Rational Mutagenesis reveal binding surface of immune adherence receptor, CR1 (CD35)

Summary for 1GKN

• Entry DOI: 10.2210/pdb1gkn/pdb
• Related: 1GKG
• Descriptor: COMPLEMENT RECEPTOR TYPE 1 (1 entity in total)
• Functional Keywords: complement, module, scr
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Membrane; Single-pass type I membrane protein: P17927
• Total number of polymer chains: 1
• Total formula weight: 14213.23

Authors

Smith, B.O.,Mallin, R.L.,Krych-Goldberg, M.,Wang, X.,Hauhart, R.E.,Bromek, K.,Uhrin, D.,Atkinson, J.P.,Barlow, P.N. (deposition date: 2001-08-16, release date: 2002-04-18, Last modification date: 2024-10-23)

Primary citation

Smith, B.O.,Mallin, R.L.,Krych-Goldberg, M.,Wang, X.,Hauhart, R.E.,Bromek, K.,Uhrin, D.,Atkinson, J.P.,Barlow, P.N.
Structure of the C3B Binding Site of Cr1 (Cd35), the Immune Adherence Receptor
Cell(Cambridge,Mass.), 108:769-, 2002

PubMed Abstract: Complement receptor type 1 (CR1 or CD35) is a multiple modular protein that mediates the immune adherence phenomenon, a fundamental event for destroying microbes and initiating an immunological response. It fulfills this role through binding C3b/C4b-opsonized foreign antigens. The structure of the principal C3b/C4b binding site (residues 901-1095) of CR1 is reported, revealing three complement control protein modules (modules 15-17) in an extended head-to-tail arrangement with flexibility at the 16-17 junction. Structure-guided mutagenesis identified a positively charged surface region on module 15 that is critical for C4b binding. This patch, together with basic side chains of module 16 exposed on the same face of CR1, is required for C3b binding. These studies reveal the initial structural details of one of the first receptor-ligand interactions to be identified in immunobiology.

PubMed: 11955431
DOI: 10.1016/S0092-8674(02)00672-4

Experimental method

SOLUTION NMR