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. 2019 Dec 26;19:1249. doi: 10.1186/s12885-019-6378-6

Correction to: Exploration for novel inhibitors showing back-to-front approach against VEGFR-2 kinase domain (4AG8) employing molecular docking mechanism and molecular dynamics simulations

Shailima Rampogu 1, Ayoung Baek 1, Amir Zeb 1, Keun Woo Lee 1,
PMCID: PMC6933660  PMID: 31878898

Correction to: BMC Cancer (2018) 18:264

https://doi.org/10.1186/s12885-018-4050-1

Following publication of the original article [1], the authors reported errors in Fig. 3, Fig. 14a, Fig. 18, Fig. 19b, Additional file 3 and Additional file 7. The title of Additional file 9 contains a typing error and is correctly given below.

Fig. 3.

Fig. 3

Most active compound (IC50 = 0.2) mapped to all the features

Fig. 14.

Fig. 14

a Molecular interaction between the reference- protein (purple). Green dotted lines indicate the hydrogen bonds. The residues are represented in orange stick model

Fig. 18.

Fig. 18

Binding mode assessment of compounds. The co-crystal is represented in gray, reference is denoted in green and the Hit in orange. All the three follow the same pattern

Fig. 19.

Fig. 19

b Intermolecular interactions between the ligand and the protein. Green dotted lines represent the hydrogen bonds. The protein residues are indicated in cyan

The following typing errors have been identified:

Page no Column/paragraph line Present word Change to
1 Abstract/results 2 of above
2 1/2 2 Cyclic Cyclin
2 2/1 3 VEGFR VEGFR-2
12 2/1 3 prognosis progression
12 2/1 10 form from
19 Above conclusions 4 Cyc919 Cys919
10 2/1 13 20 ps 20 ns
10 2/1 15 25 ps 25 ns
13 2/1 6 four five
Table 5/ reference van der Waals interactions asn900leu1044 Asn900, Ile1044
Fig 10 30 ps 30 ns
Fig 16 refrence reference

Further to this, in Table 1, HyP is incorrectly represented as HyB and Hy-Ali as HyAli/HY-Ali. The corrected Table 1 can be found here.

Table 1

Hypo no Total costa Cost difference RMSDb Correlation Featuresc Max fit
Hypo1 111.95 71.22 0.7 0.97 Hy-Ali, 2HyP,RA 11.4
Hypo 2 113.31 69.86 0.7 0.96 Hy-Ali, 2HyP,RA 11.5
Hypo 3 116.45 66.71 0.8 0.95 Hy-Ali,HyP,RA,HBA 11.9
Hypo 4 116.47 66.69 1.0 0.94 HBA, HBD 2HyP 10.7
Hypo 5 117.11 66.05 0.9 0.94 Hy-Ali,HyP,RA,HBA 11.5
Hypo 6 119.51 63.65 1.0 0.93 HBA,HBD,2HyP 11.26
Hypo 7 119.52 63.65 0.9 0.95 HBA,2HyP,RA 12.65
Hypo 8 119.82 63.35 0.9 0.94 HBA,Hy-Ali,HBD,RA 12.33
Hypo 9 119.94 63.23 1.2 0.91 HBA,Hy-Ali,2HyP, RA 11.98
Hypo10 120.52 62.65 1.1 0.91 HBA,HBD, Hy-Ali 7.8

These corrections do not alter the context of the manuscript.

Supplementary information

12885_2019_6378_MOESM1_ESM.docx (508.2KB, docx)

Additional file 3. 2D interaction representation of the reference compound and 4AG8. Detailed molecular interactions of the reference compound.

12885_2019_6378_MOESM2_ESM.docx (102.5KB, docx)

Additional file 7. 2D interaction representation of the reference compound and 1URW. Molecular interaction details of the reference compound.

12885_2019_6378_MOESM3_ESM.docx (13.9KB, docx)

Additional file 9. Active sites comparison. Comparison of the active site residues of 4AG8 and 1URW.

Supplementary information

Supplementary information accompanies this paper at 10.1186/s12885-019-6378-6.

Reference

  • 1.Rampogu S, et al. Exploration for novel inhibitors showing back-to-front approach against VEGFR-2 kinase domain (4AG8) employing molecular docking mechanism and molecular dynamics simulations. BMC Cancer. 2018;18:264. doi: 10.1186/s12885-018-4050-1. [DOI] [PMC free article] [PubMed] [Google Scholar]

Associated Data

This section collects any data citations, data availability statements, or supplementary materials included in this article.

Supplementary Materials

12885_2019_6378_MOESM1_ESM.docx (508.2KB, docx)

Additional file 3. 2D interaction representation of the reference compound and 4AG8. Detailed molecular interactions of the reference compound.

12885_2019_6378_MOESM2_ESM.docx (102.5KB, docx)

Additional file 7. 2D interaction representation of the reference compound and 1URW. Molecular interaction details of the reference compound.

12885_2019_6378_MOESM3_ESM.docx (13.9KB, docx)

Additional file 9. Active sites comparison. Comparison of the active site residues of 4AG8 and 1URW.


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