Gamma lens crystallin is one of many crystalline proteins found in lens cells of the vertebrate eye. Unlike some other lens crystallins, which seem to have been derived from various respiratory enzymes, this one has no known function other than that of being a lens protein. Like Calmodulin, Gamma-crystallin is a strophic structure, divided into four similar units with the organization beta-turn-beta-turn beta. Click here to hear the beta themes. The two halves of the protein are connected by a four-residue connecting peptide. Although the sequences of the beta strands are not obviously similar, each is characterized by octave skips between soluble residues like D, E, R, and K, and insoluble ones like V, M, I, L, F, e.g. adjacent combinations like KI, RV, RM, RF, EL. The beta sections of several species are played together in one section of the piece to demonstrate the extent to which these regions have been evolutionarily conserved.
Gamma Crystallin
B |
G [KITFY] EDR {AF} QGR [SYEC] TTDCPNLQ {PY} FSRCN [SIRVES] GC [WMIYER] {PNY} [QGHQYFL] RR [GEY] PD(YQQ) {WM} GLSDSIR [SCCL] IPP -HSGA- Y [RMKIYDR] {DEL} [RGQMSEL] TDDCLS(VQDRF)HLTEIH [SLNVLE] GS [WILYEM] {PNY} [RGRQYLL] RP [GEY] RR {FLDWG} APNAKVG [SLRR] VMDLY |