CRDs of the seven lectins showing the key conserved amino acid residues on the β strands.

• Main Authors: Ashalatha Sreshty Mamidi (7426607), Avadhesha Surolia (78297)
• Format: Still Image
• Language: unknown
• Published: 2022
• Subjects: Biophysics; Biochemistry; Cell Biology; Genetics; Molecular Biology; Evolutionary Biology; Cancer; Computational Biology; Biological Sciences not elsewhere classified; Chemical Sciences not elsewhere classified; two competing theories; similar structural architectures; several conformations spanning; reducing end glucose; provide valuable insight; conserved functional roles; explain biomolecular recognition; carbohydrate recognition domain; protein folding process; noncovalent bond interactions; molecular interaction fields; bound forms demonstrated; central mannose residues; molecular recognition process; conformational selection followed; proteins </ p; favorable lectin conformation; molecular recognition; conformational selection; specific interactions; protein sequence; also demonstrated; trp residues; key residues; conformational changes; xlink ">; since exploring; scientific scrutiny; molecular structure; mmpbsa approach; ligand binding; initially driven; induced fluctuations; induced fit; hydrophobic potentials; fundamental question; atomistic simulations; &# 8220; Canis lupus
• Online Access: https://doi.org/10.1371/journal.pcbi.1010661.g002

(A) Calnexin of Canis lupus (dog); (B) Calnexin of Humans; (C) Calmegin from Humans; (D) Calreticulin from Humans; (E) Calsperin from Humans; (F) Calreticulin from Entamoeba histolytica and (G) Calreticulin from Trypanosoma cruzi . Polar amino acids are shown in green and non-polar amino acids in red.