1A6S

M-DOMAIN FROM GAG POLYPROTEIN OF ROUS SARCOMA VIRUS, NMR, 20 STRUCTURES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 1000 
  • Conformers Submitted: 20 
  • Selection Criteria: LEAST RESTRAINT VIOLATION 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus

McDonnell, J.M.Fushman, D.Cahill, S.M.Zhou, W.Wolven, A.Wilson, C.B.Nelle, T.D.Resh, M.D.Wills, J.Cowburn, D.

(1998) J Mol Biol 279: 921-928

  • DOI: https://doi.org/10.1006/jmbi.1998.1788
  • Primary Citation of Related Structures:  
    1A6S

  • PubMed Abstract: 

    A biologically active construct of the retroviral M domain from the avian Rous sarcoma virus is defined and its solution structure described. This M domain is fully active in budding and infectivity without myristylation. In spite of a sequence homology level that suggests no relationship among M domains and the family of matrix proteins in mammalian retroviruses, the conserved structural elements of a central core allow an M domain sequence motif to be described for all retroviruses. The surface of the M domain has a highly clustered positive patch comprised of sequentially distant residues. An analysis of the backbone dynamics, incorporating rotational anisotropy, is used to estimate the thermodynamics of proposed domain oligomerization.


  • Organizational Affiliation

    The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GAG POLYPROTEIN87Rous sarcoma virus - Prague CMutation(s): 0 
Gene Names: GAG
Membrane Entity: Yes 
UniProt
Find proteins for P03322 (Rous sarcoma virus subgroup C (strain Prague))
Explore P03322 
Go to UniProtKB:  P03322
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03322
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 1000 
  • Conformers Submitted: 20 
  • Selection Criteria: LEAST RESTRAINT VIOLATION 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-10-14
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Data collection, Database references, Derived calculations, Other
  • Version 1.4: 2024-05-22
    Changes: Data collection