Folding and conformational studies on SCR1-3 domains of human complement receptor 1.


Abstract

Short consensus repeats SCR3 and SCR1-3 are soluble recombinant proteins, consisting of the third and first three N-terminal domains of complement receptor 1, respectively, which retain some anti-complement activity. The conformational stabilities and folding/unfolding of SCR3 and SCR1-3 have been studied using circular dichroism and equilibrium and pre-equilibrium fluorescence spectroscopy. Denaturation by guanidinium hydrochloride (GdnHCl) is rapid and completely reversible. Reduction of disulphide bridges in the folded proteins by beta-mercaptoethanol leads to an increase in fluorescence intensity. The fluorescence intensity of the folded proteins is approximately 7.5% of that of the respective unfolded proteins. The data can be approximated to a two-state transition between native and denatured forms of the proteins. SCR3 has a conformational stability in water of 12-13 kJ/mol whereas that of SCR1-3 is 19.5-19.9 kJ/mol depending upon the technique utilized. The heat capacity change associated with the unfolding of SCR1-3 was obtained by a series of GdnHCl unfolding experiments over a range of temperatures and was found to be 6.6 kJ/K.mol or 33.8 J/K.mol(residue). The refolding process of SCR3 was found to be simple, described by a single exponential equation, whereas that of SCR1-3 was found to be complex and could be fitted to a double exponential equation indicating the presence of folding intermediates. Study holds ProTherm entries: 10884, 10885, 10886, 10887, 10888 Extra Details: -S-S- oxidized conformation; folding; human complement receptor 1;,SCR1-3 domains

Submission Details

ID: 28GdhFot3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:41 p.m.

Version: 1

Publication Details
Clark NS;Dodd I;Mossakowska DE;Smith RA;Gore MG,Protein Eng. (1996) Folding and conformational studies on SCR1-3 domains of human complement receptor 1. PMID:8931127
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
2Q7Z 2007-10-16 Solution Structure of the 30 SCR domains of human Complement Receptor 1
1PPQ 2004-05-04 NMR structure of 16th module of Immune Adherence Receptor, Cr1 (Cd35)
2MCY 2013-11-13 CR1 Sushi domains 2 and 3
2MCZ 2013-11-13 CR1 Sushi domains 1 and 2
1GKG 2002-04-18 Structure Determination and Rational Mutagenesis reveal binding surface of immune adherence receptor, CR1 (CD35)
1GKN 2002-04-18 Structure Determination and Rational Mutagenesis reveal binding surface of immune adherence receptor, CR1 (CD35)
5FO9 2016-04-06 3.3 Crystal Structure of Human Complement C3b in Complex with CR1 (CCP15- 17)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Complement receptor type 1 P17927 CR1_HUMAN