Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily.


Abstract

The role of conserved proline residues in fibronectin type III (fnIII) domains is investigated. Surprisingly, none of the standard set of explanations for residue conservation applies. The proline residues are not apparently conserved for function, or stability, or to nucleate folding, or to promote stabilising interactions across domain boundaries. However, when the most highly conserved proline residues are mutated to alanine there is an increase in the rate of aggregation of a fnIII double-module construct. The results suggest that proline residues may be conserved at domain-domain boundaries in fnIII domains to prevent aggregation in multi-modular proteins. Study holds ProTherm entries: 15248, 15249 Extra Details: fibronectin type III; proline; protein stability; protein folding; domain-domain interactions

Submission Details

ID: gXskogWw3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:46 p.m.

Version: 1

Publication Details
Steward A;Adhya S;Clarke J,J. Mol. Biol. (2002) Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily. PMID:12054791
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
1E88 2000-09-18T00:00:00+0000 0 Solution structure of 6F11F22F2, a compact three-module fragment of the gelatin-binding domain of human fibronectin
1E8B 2000-09-18T00:00:00+0000 0 Solution structure of 6F11F22F2, a compact three-module fragment of the gelatin-binding domain of human fibronectin
1FBR 1995-08-08T00:00:00+0000 0 FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE PAIR
1FNA 1994-01-11T00:00:00+0000 1.8 CRYSTAL STRUCTURE OF THE TENTH TYPE III CELL ADHESION MODULE OF HUMAN FIBRONECTIN
1FNF 1995-09-30T00:00:00+0000 2.0 FRAGMENT OF HUMAN FIBRONECTIN ENCOMPASSING TYPE-III REPEATS 7 THROUGH 10
1FNH 1999-01-28T00:00:00+0000 2.8 CRYSTAL STRUCTURE OF HEPARIN AND INTEGRIN BINDING SEGMENT OF HUMAN FIBRONECTIN
1J8K 2001-05-22T00:00:00+0000 0 NMR STRUCTURE OF THE FIBRONECTIN EDA DOMAIN, NMR, 20 STRUCTURES
1O9A 2002-12-11T00:00:00+0000 0 Solution structure of the complex of 1F12F1 from fibronectin with B3 from FnBB from S. dysgalactiae
1OWW 2003-03-31T00:00:00+0000 0 Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy
1Q38 2003-07-28T00:00:00+0000 0 Anastellin

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
96.8 Fibronectin P07589 FINC_BOVIN
100.0 Fibronectin P02751 FINC_HUMAN
90.9 Fibronectin Q91400 FINC_NOTVI
92.1 Fibronectin Q28377 FINC_HORSE
94.0 Fibronectin Q28275 FINC_CANLF