Comparative thermodynamic study of pepsinogen and pepsin structure.


Abstract

Study holds ProTherm entries: 11204, 11205, 11206, 11207, 11208, 11209, 11210, 11211, 11212, 11213, 11214, 11215, 11216, 11217, 11218, 11219, 11220, 11221, 11222, 11223, 11224, 11225, 11226, 11227, 11228 Extra Details: two-state transition; co-operative units; domains

Submission Details

ID: mnnoDmqN3

Submitter: Connie Wang

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

Version: 1

Publication Details
Privalov PL;Mateo PL;Khechinashvili NN;Stepanov VM;Revina LP,J. Mol. Biol. (1981) Comparative thermodynamic study of pepsinogen and pepsin structure. PMID:6799654
Additional Information

Study Summary

Number of data points 73
Proteins Pepsin A ; Gastricsin ; Pepsin A ; Pepsin A
Unique complexes 2
Assays/Quantities/Protocols Experimental Assay: dHcal pH:7.5, ionic:NaCl: 100 mM, buffers:sodium phosphate: 5 mM ; Experimental Assay: Tm pH:7.5, ionic:NaCl: 100 mM, buffers:sodium phosphate: 5 mM ; Experimental Assay: dHvH pH:7.5, ionic:NaCl: 100 mM, buffers:sodium phosphate: 5 mM ; Experimental Assay: dHcal pH:7.5, buffers:sodium phosphate: 5 mM, ionic:: ; Experimental Assay: Tm pH:7.5, buffers:sodium phosphate: 5 mM, ionic:: ; Experimental Assay: dHvH pH:7.5, buffers:sodium phosphate: 5 mM, ionic:: ; Experimental Assay: dHcal ionic:NaCl: 10 mM, buffers:sodium phosphate: 5 mM, pH:7.1 ; Experimental Assay: Tm ionic:NaCl: 10 mM, buffers:sodium phosphate: 5 mM, pH:7.1 ; Experimental Assay: dHvH ionic:NaCl: 10 mM, buffers:sodium phosphate: 5 mM, pH:7.1 ; Experimental Assay: dHcal ionic:NaCl: 100 mM, buffers:sodium cacodylate: 5 mM, pH:5.9 ; Experimental Assay: Tm ionic:NaCl: 100 mM, buffers:sodium cacodylate: 5 mM, pH:5.9 ; Experimental Assay: dHvH ionic:NaCl: 100 mM, buffers:sodium cacodylate: 5 mM, pH:5.9 ; Experimental Assay: dHcal ionic:: , buffers:sodium cacodylate: 5 mM, pH:5.9 ; Experimental Assay: Tm ionic:: , buffers:sodium cacodylate: 5 mM, pH:5.9 ; Experimental Assay: dHvH ionic:: , buffers:sodium cacodylate: 5 mM, pH:5.9 ; Experimental Assay: dHcal buffers:sodium phosphate: 5 mM, ionic:: , pH:6.5 ; Experimental Assay: Tm buffers:sodium phosphate: 5 mM, ionic:: , pH:6.5 ; Experimental Assay: dHvH buffers:sodium phosphate: 5 mM, ionic:: , pH:6.5 ; Experimental Assay: dHcal pH:7.1, ionic:NaCl: 100 mM, buffers:sodium phosphate: 5 mM ; Experimental Assay: Tm pH:7.1, ionic:NaCl: 100 mM, buffers:sodium phosphate: 5 mM ; Experimental Assay: dHvH buffers:sodium phosphate: 5 mM, ionic:NaCl: 100 mM, pH:7.1 ; Experimental Assay: dHcal buffers:sodium phosphate: 5 mM, ionic:: , pH:8.0 ; Experimental Assay: Tm buffers:sodium phosphate: 5 mM, ionic:: , pH:8.0 ; Experimental Assay: dHvH buffers:sodium phosphate: 5 mM, ionic:: , pH:8.0 ; Experimental Assay: dHcal pH:7.1, buffers:sodium phosphate: 5 mM, ionic:: ; Experimental Assay: Tm pH:7.1, buffers:sodium phosphate: 5 mM, ionic:: ; Experimental Assay: dHvH ionic:: , buffers:sodium phosphate: 5 mM, pH:7.1 ; Experimental Assay: dHcal ionic:NaCl: 100 mM, buffers:sodium phosphate: 5 mM, pH:6.5 ; Experimental Assay: Tm ionic:NaCl: 100 mM, buffers:sodium phosphate: 5 mM, pH:6.5 ; Experimental Assay: dHvH ionic:NaCl: 100 mM, buffers:sodium phosphate: 5 mM, pH:6.5 ; Experimental Assay: dHcal pH:6.0, ionic:: , buffers:sodium cacodylate: 5 mM ; Experimental Assay: Tm pH:6.0, ionic:: , buffers:sodium cacodylate: 5 mM ; Experimental Assay: dHvH pH:6.0, ionic:: , buffers:sodium cacodylate: 5 mM
Libraries Mutations for sequence IGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIASLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA ; Mutations for sequence LVKVPLVRKKSLRQNLIKDGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTIDGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA

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
3PSG 1993-01-15 1.65 THE HIGH RESOLUTION CRYSTAL STRUCTURE OF PORCINE PEPSINOGEN
2PSG 1992-10-15 1.8 REFINED STRUCTURE OF PORCINE PEPSINOGEN AT 1.8 ANGSTROMS RESOLUTION
4PEP 1990-04-15 1.8 THE MOLECULAR AND CRYSTAL STRUCTURES OF MONOCLINIC PORCINE PEPSIN REFINED AT 1.8 ANGSTROMS RESOLUTION
3PEP 1990-04-15 2.3 REVISED 2.3 ANGSTROMS STRUCTURE OF PORCINE PEPSIN. EVIDENCE FOR A FLEXIBLE SUBDOMAIN
5PEP 1990-07-15 2.34 X-RAY ANALYSES OF ASPARTIC PROTEASES. II. THREE-DIMENSIONAL STRUCTURE OF THE HEXAGONAL CRYSTAL FORM OF PORCINE PEPSIN AT 2.3 ANGSTROMS RESOLUTION
1F34 2001-02-01 2.45 CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN
1PSA 1994-01-31 2.9 STRUCTURE OF A PEPSIN(SLASH)RENIN INHIBITOR COMPLEX REVEALS A NOVEL CRYSTAL PACKING INDUCED BY MINOR CHEMICAL ALTERATIONS IN THE INHIBITOR
1YX9 2005-05-24 3.0 Effect of Dimethyl Sulphoxide on the crystal structure of Porcine Pepsin

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Pepsin A P00791 PEPA_PIG
100.0 Gastricsin P30879 PEPC_PIG