Review




Structured Review

InterPro Inc alphafold2 software program
Modeled structure of the RhoGAP domains of ArhGAP21, ArhGAP23, and DmRhoGAP19D. (a) Schematic representation of ArhGAP21 and ArhGAP23 (orange box: PDZ domain, blue box: PH domain, green box: RhoGAP domain). UniProt and GenBank IDs are as follows: ArhGAP21: Q5T5U3-1/NM_20824.4; ArhGAP23: Q9P227-1/NM_001199417.2; and DmRhoGAP19D: Q9VRA6/NM_134552.6. (b) Modeled structure of the RhoGAP domain by homology modeling. RhoGAP domains are colored from the N-terminus (blue) to the C-terminus (red). (c) The modeled structure of the ArhGAP21 domain was superimposed over the RhoGAP domain of ArhGAP23. (d) Modeled structure of the RhoGAP domain generated by <t>AlphaFold2.</t> (e) The modeled structure of the ArhGAP21 RhoGAP domain was superimposed over the RhoGAP domain of ArhGAP23. The modeled structure was evaluated by PROCHECK and ERRAT and visualized by the UCSF Chimera software program, version 1.15 ( http://www.cgl.ucsf.edu/chimera ).
Alphafold2 Software Program, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Images

1) Product Images from "A Structural Network Analysis of Neuronal ArhGAP21/23 Interactors by Computational Modeling"

Article Title: A Structural Network Analysis of Neuronal ArhGAP21/23 Interactors by Computational Modeling

Journal: ACS Omega

doi: 10.1021/acsomega.2c08054

Modeled structure of the RhoGAP domains of ArhGAP21, ArhGAP23, and DmRhoGAP19D. (a) Schematic representation of ArhGAP21 and ArhGAP23 (orange box: PDZ domain, blue box: PH domain, green box: RhoGAP domain). UniProt and GenBank IDs are as follows: ArhGAP21: Q5T5U3-1/NM_20824.4; ArhGAP23: Q9P227-1/NM_001199417.2; and DmRhoGAP19D: Q9VRA6/NM_134552.6. (b) Modeled structure of the RhoGAP domain by homology modeling. RhoGAP domains are colored from the N-terminus (blue) to the C-terminus (red). (c) The modeled structure of the ArhGAP21 domain was superimposed over the RhoGAP domain of ArhGAP23. (d) Modeled structure of the RhoGAP domain generated by AlphaFold2. (e) The modeled structure of the ArhGAP21 RhoGAP domain was superimposed over the RhoGAP domain of ArhGAP23. The modeled structure was evaluated by PROCHECK and ERRAT and visualized by the UCSF Chimera software program, version 1.15 ( http://www.cgl.ucsf.edu/chimera ).
Figure Legend Snippet: Modeled structure of the RhoGAP domains of ArhGAP21, ArhGAP23, and DmRhoGAP19D. (a) Schematic representation of ArhGAP21 and ArhGAP23 (orange box: PDZ domain, blue box: PH domain, green box: RhoGAP domain). UniProt and GenBank IDs are as follows: ArhGAP21: Q5T5U3-1/NM_20824.4; ArhGAP23: Q9P227-1/NM_001199417.2; and DmRhoGAP19D: Q9VRA6/NM_134552.6. (b) Modeled structure of the RhoGAP domain by homology modeling. RhoGAP domains are colored from the N-terminus (blue) to the C-terminus (red). (c) The modeled structure of the ArhGAP21 domain was superimposed over the RhoGAP domain of ArhGAP23. (d) Modeled structure of the RhoGAP domain generated by AlphaFold2. (e) The modeled structure of the ArhGAP21 RhoGAP domain was superimposed over the RhoGAP domain of ArhGAP23. The modeled structure was evaluated by PROCHECK and ERRAT and visualized by the UCSF Chimera software program, version 1.15 ( http://www.cgl.ucsf.edu/chimera ).

Techniques Used: Generated, Software

Related Articles

other:

Article Title: Computational Screening of Filamin Mechanical Binding Proteins using AlphaFold2
Article Snippet: Then, the InterPro-Alphafold2 model had RMSD values from 0.573 Å for Ig 19 to 1.056 Å for Ig 16.

Article Title: Computational Screening of Filamin Mechanical Binding Proteins using AlphaFold2
Article Snippet: As a control, we used the InterPro-Alphafold2 model from the InterPro database corresponding to the Filamin-PA splice variant (Q9VEN1; Cher-PA).

Article Title: PRESCOTT: a population aware, epistatic, and structural model accurately predicts missense effects
Article Snippet: E AlphaFold confidence (from InterPro) of positions in the Spastin’s structural model. Confidence is represented by a color scale from dark blue (very high) to red (very low) It should be noted that sensitive regions identified in the ESCOTT matrix are not a direct consequence of the integration of structural information into the model.

Article Title: The stomatin-like protein StlP organizes membrane microdomains to govern polar growth in filamentous actinobacteria under hyperosmotic stress
Article Snippet: Protein domains and protein structures were predicted by InterPro ( https://www.ebi.ac.uk/interpro/ ) and AlphaFold 2.0 .

Article Title: Computational Screening of Filamin Mechanical Binding Proteins using AlphaFold2
Article Snippet: Like our ColabFold-AlphaFold2 results, the InterPro model correctly predicted the closed state of the two domain pairs with high pLDDT values ( , and Supporting information - ).

Sequencing:

Article Title: A defining member of the new cysteine-cradle family is an aECM protein signalling skin damage in C. elegans.
Article Snippet: .. with AlphaFold of the 6 CCD-aECM proteins in C. elegans. (A) Domain organisation of the 6 CCD-aECM proteins in C. elegans, as annotated in InterPro [28,64] and (B) structural models predicted with AlphaFold [27,65], rendered with the Predicted Local Distance Difference Test score (pLDDT), which indicates how well a predicted protein structure matches protein data bank structure information and multiple sequence alignment data. (TIF) S3 Fig. SPIA-1::sfGFP and SPIA-1::mNG in L4 and adult. (A) The confocal image of the SPIA-1::sfGFP reporter (GFP-int) in the adult shown in Fig 4D is presented aside from a representative adult wild-type imaged using same illumination conditions; n>5, scale bar, 5 μm. (B) Zoom on the furrows in the L4.4 shown in Fig 4F. ..



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Image Search Results


Relevant hits from  AlphaFold2  predicted structures of Deep-Blue and Vp4 tail proteins submitted to the Dali server to retrieve related structures

Journal: Journal of Virology

Article Title: Deciphering the adsorption machinery of Deep-Blue and Vp4, two myophages targeting members of the Bacillus cereus group

doi: 10.1128/jvi.00745-24

Figure Lengend Snippet: Relevant hits from AlphaFold2 predicted structures of Deep-Blue and Vp4 tail proteins submitted to the Dali server to retrieve related structures

Article Snippet: Recently, the DeepMind’s machine-learning protein structure prediction program AlphaFold2 (AF2) ( ) has been proven to be extremely valuable in obtaining structures of phage tail proteins and of their complexes, as exemplified by the baseplate structure predictions of a few siphophages ( ).

Techniques: Injection, Membrane