Conformation and disulfide bond formation of the constant fragment of an immunoglobulin light chain: effect of truncation at the C-terminal region.


Abstract

Constant fragments with different carboxyl terminals, CL(109-211), CL(109-207), and CL-(109-200), were prepared by limited carboxypeptidase P or Y proteolysis of the constant fragment, CL-(109-214), of a type lambda immunoglobulin light chain, and their conformations and stabilities, and formation of the disulfide bond from the reduced fragments, were studied. No change in conformation or stability was observed on removal of three residues from the C-terminal end. Removal of seven or more residues from the C-terminal end destabilized the CL fragment. The rate of disulfide bond formation from reduced CL(109-207) was about 7 times faster than that for CL(109-214). These findings suggest that elongation of the polypeptide chain at least beyond the 207th residue is necessary for folding of the CL fragment into a definite conformation. Study holds ProTherm entries: 3982, 3983, 3984, 3985, 3986, 3987 Extra Details: constant fragments; conformations; disulfide bond; stability

Submission Details

ID: JLYZ9aaX3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:23 p.m.

Version: 1

Publication Details
Ishiwata A;Kawata Y;Hamaguchi K,Biochemistry (1991) Conformation and disulfide bond formation of the constant fragment of an immunoglobulin light chain: effect of truncation at the C-terminal region. PMID:1907845
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
1AR2 1997-08-08T00:00:00+0000 2.8 DISULFIDE-FREE IMMUNOGLOBULIN FRAGMENT
1BWW 1998-09-29T00:00:00+0000 1.7 BENCE-JONES IMMUNOGLOBULIN REI VARIABLE PORTION, T39K MUTANT
1REI 1976-03-17T00:00:00+0000 2.0 THE MOLECULAR STRUCTURE OF A DIMER COMPOSED OF THE VARIABLE PORTIONS OF THE BENCE-JONES PROTEIN REI REFINED AT 2.0 ANGSTROMS RESOLUTION
1WTL 1994-06-08T00:00:00+0000 1.9 COMPARISON OF CRYSTAL STRUCTURES OF TWO HOMOLOGOUS PROTEINS: STRUCTURAL ORIGIN OF ALTERED DOMAIN INTERACTIONS IN IMMUNOGLOBULIN LIGHT CHAIN DIMERS
4L1H 2013-06-03T00:00:00+0000 1.68 Bence-Jones immunoglobulin REI variable portion with seven point mutations
5XP1 2017-05-31T00:00:00+0000 2.88 Structure of monomeric mutant of REI immunoglobulin light chain variable domain crystallized at pH 6
1EEQ 2000-02-01T00:00:00+0000 1.5 M4L/Y(27D)D/T94H Mutant of LEN
1EEU 2000-02-03T00:00:00+0000 1.6 M4L/Y(27D)D/Q89D/T94H mutant of LEN
1EFQ 2000-02-09T00:00:00+0000 1.6 Q38D mutant of LEN
1EK3 2000-03-06T00:00:00+0000 1.9 KAPPA-4 IMMUNOGLOBULIN VL, REC

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Immunoglobulin kappa variable 1D-33 P01593 KVD33_HUMAN
100.0 Immunoglobulin kappa variable 1D-33 P01594 KV133_HUMAN
99.0 Immunoglobulin kappa variable 4-1 P06312 KV401_HUMAN