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. 2013 Aug 6;8(8):e70336. doi: 10.1371/journal.pone.0070336

Table 1. Summary of the structural analysis of various mutants of human γD crystallin.

S.No. Mutants Secondary structure and solvent accessibility of the residue Non polar residues with increased solvent exposure in the mutant* Polar residues with increased solvent exposure in the mutant* Effect on Inter-domain interactions Intermolecular interactions at the site of mutation
1 P24T Edge strand in the second Greek key (GK) motif in the N-terminal domain is solvent-exposed Y6,Y16,Y45,Y50,Y62, A63,Y98,F118,W157,A159 T4,E7,R9,Q12,R14,H15,E17,D21,P23),S30,N33,R36,D38,Y45,Q47,S51,R59,D61,H65Q66,Q67,S72,D73,R76,S87,H88,R89,R95,R99,Q101,C111,Q113,R115,N125,E128,R140,T160,R163 Indirectly Not directly affected
A36P GK-1motif disturb due to Proline P43,L53, F118,F173 R9,N33, C41,Q47, H65,Q66, D 97,R99,C111, GK1 not involved in interdomain interactions. However, the conformation change and destabilization of GK1 might indirectly affect. Altered stability and conformation of the GK1 might affect Intermolecular interactions
3 L45PL54P Residues are in the middle and edge strands, respectively, in GK 2. L45 is buried, L54 is solvent-exposed L53, M69, L71, R9, E46, D64, Q66, Q67, S74, R76, R99 GK2 involved in domain-domain interactions. The conformation and stability of this β sheet is affected due to the presence of prolines Altered stability and conformation of the GK2 might affect Intermolecular interactions
4 R77S One of the middle strands in GK motif 2 in N-terminal domain is solvent -exposed Y55, F118, I171 R9, F24, Q26, N33, E46,Q47,N49,Q66,Q67,S72,S74,S77,D97,R99,Q101 No Occurs close to a positively charged patch in symmetry- related molecule
5 E107A Loop connecting the two GKs in C-terminal domain, solvent-exposed L53,F105,F118 R9,N33,Q66,R76,H88,R89, D97,R99,Q101,T106,D108,C109,R169 No Polar environment in the symmetry- related molecule
6 Y134A Located at the middle strand in GK4, buried L53, M69, F118, V132, Y139, R9,N33, E46, D64, N66, N67, S74, R76, D97, R99, Q101,R140, Q143 Possibly affected as the site occurs in GK4 involved in inter-domain interactions Does not seem to be affected
7 R140X Three strands corresponding to both the motifs and a loop connecting the two strands L53,F56,I81,I90,L92,Y98,L112,I121,L124,V126,L127,W131,V132,L133,Y134,L136, 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 Affected Could be affected due to unfolding of the molecule
8 W157X Loop and beta strand at the C-terminal region F56,I81,L92,L112,I121,L124,W131,V132,L133,Y134,L136,Y139,Y144,L146,Y151,Y154, Q54,R59,S84,H88,T106,D108,C109,Q113,N119,E120,S130,E135,S137,R142,Y144,Y154, #W157,A159,A162,V164,L167,V170 Affected Could be affected due to unfolding of the molecule
9 G165fs L53,F56,I81,L92,F118,W131,V132,L133,Y139, R9,N33,R59,Q66,Q67,R76,S84,H88,D97,R99,Q101,T106,D108,C109,S130,Y134,#V170 Affected Possibly affected due to unfolding
#

The residues indicated in italics are the residues buried in the WT but absent in the respective mutants.