PMID- 28672114
OWN - NLM
STAT- MEDLINE
DCOM- 20190218
LR  - 20190219
IS  - 1538-0254 (Electronic)
IS  - 0739-1102 (Linking)
VI  - 36
IP  - 9
DP  - 2018 Jul
TI  - Amaranthus caudatus lectin with polyproline II fold: conformational and 
      functional transitions and molecular dynamics.
PG  - 2203-2215
LID - 10.1080/07391102.2017.1345328 [doi]
AB  - Polyproline II (PPII) fold, a peculiar structural element was detected in the 
      Amaranthus caudatus seed lectin (ACL) based on far UV circular dichroism 
      spectrum, conformational transitions of the lectin, and a distinct isodichroic 
      point in thermal denaturation. It was confirmed using PolyprOnline database to 
      estimate the percentage of amino acids contributing to PPII fold and showed the 
      values as 13.5 and 13.9% for PROSS and XTLSSTR, respectively. Investigations of 
      the functional and conformational transitions of ACL during thermal-, pH-, and 
      guanidine hydrochloride (GdnHCl)-induced denaturation were carried out using 
      biochemical and biophysical techniques and molecular dynamics (MD) simulations 
      approach. The lectin got aggregated at 60 degrees C with instantaneous structural 
      alterations. The aggregation-prone regions in ACL were predicted using online 
      servers viz. AGGRESCAN, AmylPred, FoldAmyloid, and Waltz that were represented by 
      Visual Molecular Dynamics tools. Nine conserved regions were identified by these 
      softwares as being 'hot-spots' for aggregation. MD simulation studies of the 
      lectin at 60 degrees C revealed increase in radius of gyration. The loss of PPII fold in 
      2.0 M GdnHCl was reversible. The partially unfolded intermediate of ACL with 
      diminished PPII fold formed at pH 1.0 was stable up to 90 degrees C. The polyproline II 
      fold has been rarely detected in lectins, ACL being the second after the potato 
      lectin.
FAU - Yadav, Priya
AU  - Yadav P
AD  - a Academy of Scientific and Innovative Research (AcSIR) NCL campus, Biochemical 
      Sciences Division , CSIR-NCL , Pune , India.
AD  - b Biochemical Sciences Division , CSIR-National Chemical Laboratory , Dr Homi 
      Bhabha Road, Pune 411008 , India.
FAU - Shahane, Ganesh
AU  - Shahane G
AD  - c Institute of Bioengineering, Queen Mary University of London , Mile End Road, 
      London , UK.
FAU - Gaikwad, Sushama
AU  - Gaikwad S
AD  - b Biochemical Sciences Division , CSIR-National Chemical Laboratory , Dr Homi 
      Bhabha Road, Pune 411008 , India.
LA  - eng
PT  - Journal Article
DEP - 20170706
PL  - England
TA  - J Biomol Struct Dyn
JT  - Journal of biomolecular structure & dynamics
JID - 8404176
RN  - 0 (Amino Acids)
RN  - 0 (Lectins)
RN  - 0 (Peptides)
RN  - 0 (Protein Aggregates)
RN  - 0 (lectin, Amaranthus caudatus)
RN  - 25191-13-3 (polyproline)
SB  - IM
MH  - Amino Acids
MH  - Hemagglutination
MH  - Hemagglutination Tests
MH  - Hydrogen-Ion Concentration
MH  - Lectins/*chemistry
MH  - Molecular Conformation
MH  - *Molecular Dynamics Simulation
MH  - Peptides/*chemistry
MH  - Protein Aggregates
MH  - Protein Denaturation
MH  - *Protein Folding
MH  - Quantitative Structure-Activity Relationship
MH  - Spectrum Analysis
MH  - Temperature
OTO - NOTNLM
OT  - Amaranthus caudatus seed lectin
OT  - MD simulations
OT  - molten globule
OT  - polyproline II fold
OT  - thermal aggregation
EDAT- 2017/07/04 06:00
MHDA- 2019/02/20 06:00
CRDT- 2017/07/04 06:00
PHST- 2017/07/04 06:00 [pubmed]
PHST- 2019/02/20 06:00 [medline]
PHST- 2017/07/04 06:00 [entrez]
AID - 10.1080/07391102.2017.1345328 [doi]
PST - ppublish
SO  - J Biomol Struct Dyn. 2018 Jul;36(9):2203-2215. doi: 
      10.1080/07391102.2017.1345328. Epub 2017 Jul 6.