Q26, N33, E46,Q47,N49, Q66,Q67,S72,S74,S77,D97,R99,Q101 R9,N33,Q66,R76,H88,R89, D97,R99, Q101,T106,D108,C109,R169 R9,N33, E46, D64, N66, N67, S74, R76, D97, R99, Q101,R140, Q143 Y45,Q54,R59,R79,S84,H88,E96,D97, Y98,T106,D108,C109,Q113,N119,E120, H122,N125,S130,E135,S137,N138, #Y144,L145,L146,W157,A159,A162, V164,L167,V170 Q54,R59,S84,H88,T106,D108,C109, Q113,N119,E120,S130,E135,S137, R142,Y144,Y154, #W157,A159,A162, V164,L167,V170 R9,N33,R59,Q66,Q67,R76,S84,H88,D97,R99, Q101,T106,D108,C109,S130,Y134,#V170 No L53,F105,F118 L53, M69, F118, V132, Y139, L53,F56,I81,I90,L92,Y98,L112, I121,L124,V126,L127,W131,V132, L133,Y134,L136, Possibly affected as the web site happens in GK4 involved in inter-domain interactions Affected Doesn’t appear to be impacted F56,I81,L92,L112,I121,L124,W131, V132,L133,Y134,L136,Y139,Y144, L146,Y151,Y154, L53,F56,I81,L92,F118,W131,V132, L133,Y139, Impacted Affected Possibly impacted on account of unfoldingTable 1. Summary of your structural analysis of several mutants of human cD crystallin.S.No.MutantsSecondary structure and Non polar residues with solvent accessibility in the improved solvent exposure in Polar residues with enhanced solvent residue the mutant* exposure in the mutant*P24TEdge strand inside the second Greek essential (GK) motif in the N-terminal domain is solvent-exposedA36PGK-1motif disturb as a consequence of ProlineL45PL54PResidues are within the middle L53, M69, L71, and edge strands, respectively, in GK 2. L45 is buried, L54 is solvent-exposedR77SOne on the middle strands in GK motif 2 in N-terminal domain is solvent -exposedOccurs close to a positively charged patch in symmetry- connected molecule Polar atmosphere in the symmetryrelated moleculeE107ALoop connecting the two GKs in C-terminal domain, solvent-exposedY134ALocated in the middle strand in GK4, buriedR140XThree strands corresponding to both the motifs and a loop connecting the two strandsCould be impacted as a consequence of unfolding from the moleculeW157XLoop and beta strand at the C-terminal regionCould be impacted due to unfolding from the moleculeG165fsGreek Key Motif and Central Eye Lens Transparency# The residues indicated in italics will be the residues buried within the WT but absent within the respective mutants.Lurtotecan Purity & Documentation doi:ten.SQ109 In Vitro 1371/journal.PMID:23613863 pone.0070336.tGreek Key Motif and Central Eye Lens TransparencyFigure 5. Modeled structures of HGDC and mutants. The residues with enhanced nonpolar surface exposed to the solvent are indicated in magenta, and polar residues indicated in green; the internet site of mutation is highlighted in black. doi:10.1371/journal.pone.0070336.gTable S1 in File S1 also lists the mutations reported in human cCand cS- crystallins and also the related cataract kinds. Here again we notice the nuclear-peripheral dichotomy. The N-terminal domain mutants T5P and Gfs62 (neither disturbing the Greek essential motif ) in human cC- crystallin are linked having a Coppock-type cataract and zonular pulverulant cataract, respectively, although C109X, S119S (actually a polymorphism), and W157X (all of which disturb the Greek crucial fold) generate nuclear cataracts. R168W, which doesn’t have an effect on the Greek key, causes lamellar cataract. Turning to human cS-crystallin, 4 mutations in this molecule have so far been reported, all in the N-terminal domain, i.e., G18V, D26G, S39C and V42M. Neither G18V [46,47] nor D26G (our own unpublished outcomes) alter the motif and are related with peripheral cataracts, as also S39C though its structural analysis isn’t reported but. V42M is reported to become associated with de.
