In enteroviruses,<unk>  prevents the virus from exposing its RNA, and in rhinoviruses<unk>  prevents the virus from attaching itself to the host cell. Human rhinoviruses (HRVs) contain four structural proteins labeled VP1-VP4. Proteins VP1, VP2 and VP3 are eight stranded anti-parallel β-barrels. VP4 is an extended polypeptide chain on the viral capsid inner surface.<unk>  binds to a hydrophobic pocket in the VP1 protein.<unk>  has been shown in viral assembly to associate with viral particles. Through noncovalent, hydrophobic interactions compounds can bind to the hydrophobic pocket. Amino acids in positions Tyr152 and Val191 are a part of the VP1 drug binding pocket. This Image was created in JMOL showing the beta sheets and alpha helices of the Human Rhinovirus. The molecule embedded in the hydrophobic pocket of the VP1 protein is<unk>  In Coxsackievirus,<unk>  efficiency correlates to the susceptibility of CVB3 with the amino acid at position 1092 in the hydrophobic pocket. Amino acid 1092 is in close proximity to the central ring of capsid binders. The binding of<unk>  in the hydrophobic pocket creates conformational changes, which increases the rigidity of the virion and decreases the virions' ability to interact with its receptor. Drugs bind with the methylisoxazole ring close to the entrance pocket in VP1, the 3-fluromethyl oxadiazole ring at the end of the pocket and the phenyl ring in the center of the pocket.
Pleconaril
Mitapivat
Enarodustat
Proxicromil
Lemborexant
Riociguat
Plerixafor
Avacopan