6RPV

Extremely stable monomeric variant of human cystatin C with single amino acid substitution


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

  • Method: SOLUTION SCATTERING

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with single amino acid substitution.

Maszota-Zieleniak, M.Jurczak, P.Orlikowska, M.Zhukov, I.Borek, D.Otwinowski, Z.Skowron, P.Pietralik, Z.Kozak, M.Szymanska, A.Rodziewicz-Motowidlo, S.

(2020) FEBS J 287: 361-376

  • DOI: https://doi.org/10.1111/febs.15010
  • Primary Citation of Related Structures:  
    6ROA, 6RPV

  • PubMed Abstract: 

    Human cystatin C (hCC), a member of the superfamily of papain-like cysteine protease inhibitors, is the most widespread cystatin in human body fluids. This small protein, in addition to its physiological function, is involved in various diseases, including cerebral amyloid angiopathy, cerebral hemorrhage, stroke, and dementia. Physiologically active hCC is a monomer. However, all structural studies based on crystallization led to the dimeric structure formed as a result of a three-dimensional exchange of the protein domains (3D domain swapping). The monomeric structure was obtained only for hCC variant V57N and for the protein stabilized by an additional disulfide bridge. With this study, we extend the number of models of monomeric hCC by an additional hCC variant with a single amino acid substitution in the flexible loop L1. The V57G variant was chosen for the X-ray and NMR structural analysis due to its exceptional conformational stability in solution. In this work, we show for the first time the structural and dynamics studies of human cystatin C variant in solution. We were also able to compare these data with the crystal structure of the hCC V57G and with other cystatins. The overall cystatin fold is retained in the solute form. Additionally, structural information concerning the N terminus was obtained during our studies and presented for the first time. DATABASE: Crystallographic structure: structural data are available in PDB databases under the accession number 6ROA. NMR structure: structural data are available in PDB and BMRB databases under the accession numbers 6RPV and 34399, respectively.


  • Organizational Affiliation

    Faculty of Chemistry, University of Gdansk, Gdansk, Poland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cystatin-C120Homo sapiensMutation(s): 1 
Gene Names: CST3
UniProt & NIH Common Fund Data Resources
Find proteins for P01034 (Homo sapiens)
Explore P01034 
Go to UniProtKB:  P01034
PHAROS:  P01034
GTEx:  ENSG00000101439 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01034
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 
  • Method: SOLUTION SCATTERING

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Polish National Science CentrePolandUMO/2011/03/N/ST4/01293

Revision History  (Full details and data files)

  • Version 1.0: 2019-07-31
    Type: Initial release
  • Version 1.1: 2019-08-21
    Changes: Data collection, Structure summary
  • Version 1.2: 2020-01-29
    Changes: Database references
  • Version 1.3: 2023-06-14
    Changes: Database references, Other