5DAE

Kazal type inhibitor from salivary glands of Aedes aegypti mosquito


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.180 
  • R-Value Observed: 0.183 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

High-resolution structure of a Kazal-type serine protease inhibitor from the dengue vector Aedes aegypti.

Torquato, R.J.S.Lu, S.Martins, N.H.Tanaka, A.S.Pereira, P.J.B.

(2017) Acta Crystallogr F Struct Biol Commun 73: 469-475

  • DOI: https://doi.org/10.1107/S2053230X17010007
  • Primary Citation of Related Structures:  
    5DAE

  • PubMed Abstract: 

    Blood-feeding exoparasites are rich sources of protease inhibitors, and the mosquito Aedes aegypti, which is a vector of Dengue virus, Yellow fever virus, Chikungunya virus and Zika virus, is no exception. AaTI is a single-domain, noncanonical Kazal-type serine proteinase inhibitor from A. aegypti that recognizes both digestive trypsin-like serine proteinases and the central protease in blood clotting, thrombin, albeit with an affinity that is three orders of magnitude lower. Here, the 1.4 Å resolution crystal structure of AaTI is reported from extremely tightly packed crystals (∼22% solvent content), revealing the structural determinants for the observed inhibitory profile of this molecule.


  • Organizational Affiliation

    Department of Biochemistry, Escola Paulista de Medicina, Universidade Federal de São Paulo (UNIFESP), Rua 3 de Maio 100, 04044-020 São Paulo-SP, Brazil.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
AAEL006007-PA
A, B
65Aedes aegyptiMutation(s): 0 
Gene Names: AAEL006007
UniProt
Find proteins for Q1HRB8 (Aedes aegypti)
Explore Q1HRB8 
Go to UniProtKB:  Q1HRB8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ1HRB8
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.180 
  • R-Value Observed: 0.183 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 26.136α = 90
b = 65.167β = 116.5
c = 27.662γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
SCALAdata scaling
SHELXphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Sao Paulo Research Foundation (FAPESP)Brazil2012/03657-8

Revision History  (Full details and data files)

  • Version 1.0: 2016-09-07
    Type: Initial release
  • Version 1.1: 2018-09-12
    Changes: Data collection, Database references, Derived calculations
  • Version 1.2: 2019-04-17
    Changes: Author supporting evidence, Data collection
  • Version 1.3: 2020-01-01
    Changes: Author supporting evidence