X-ray diffraction and structure of crystallins

Slingsby, C.; Norledge, B.V.; Simpson, A.A.; Bateman, O.A.; Wright, G.; Driessen, H.P.C.; Lindley, P. F.; Moss, David S.; Bax, Benjamin

doi:10.1016/s1350-9462(96)00018-3

Cited by 39 publications

(28 citation statements)

References 101 publications

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“…1). Along with this signature sequence, ϳ24 -30 residues downstream, a conserved Ser is located (on the fourth ␤-strand), which plays a structural role by stabilizing this ␤-hairpin (19,20,48). The third strand of each Greek key is swapped and becomes a part of the partner Greek key motif ((3,1) arrangement of ␤-strands) (Fig.…”

Section: Architecture Of the ␤␥-Crystallin-type Ca 2؉ -Binding Motifmentioning

confidence: 99%

“…The fifth residue is usually Ser (or sometimes Thr), which coordinates via the hydroxyl oxygen and is a determinant for domain properties. The sixth nonligating residue is highly conserved structural Ser, which stabilizes the ␤-hairpin loop (48). The crystal structures of ␤␥-crystallin domains available in the Ca 2ϩ -bound form display a common theme of Ca 2ϩ coordination that led to the proposition of a distinct motif for Ca 2ϩ binding in the ␤␥-crystallin superfamily (Table 1), although some of these structures carry minor variations in this theme, which are discussed below.…”

Section: Preferred Residues In the Binding Motif And Their Significancementioning

confidence: 99%

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Ca2+-binding Motif of βγ-Crystallins

Srivastava¹,

Mishra

Krishnan³

et al. 2014

Journal of Biological Chemistry

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␤␥-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca2؉ binding. A ␤␥-crystallin domain is formed of two Greek key motifs, accommodating two Ca 2؉ -binding sites. ␤␥-Crystallins make a separate class of Ca 2؉ -binding proteins (CaBP), apparently a major group of CaBP in bacteria. Paralleling the diversity in ␤␥-crystallin domains, these motifs also show great diversity, both in structure and in function. Although the expression of some of them has been associated with stress, virulence, and adhesion, the functional implications of Ca 2؉ binding to ␤␥-crystallins in mediating biological processes are yet to be elucidated.

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Section: Architecture Of the ␤␥-Crystallin-type Ca 2؉ -Binding Motifmentioning

confidence: 99%

Section: Preferred Residues In the Binding Motif And Their Significancementioning

confidence: 99%

Ca2+-binding Motif of βγ-Crystallins

Srivastava¹,

Mishra

Krishnan³

et al. 2014

Journal of Biological Chemistry

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“…Sequencing and 3D structural studies have shown that members of the bg-crystallin superfamily are each formed from two similar compact domains joined by a short linker (Bax et al, 1990;de Jong et al, 1994;Slingsby et al, 1997). The major structural difference between the b-and g-crystallin families is the intramolecular domain pairing of the monomeric g-crystallins as contrasted with the intermolecular domain pairing of partner subunits in the dimeric bB2-crystallin.…”

Section: Introductionmentioning

confidence: 99%

Association Behaviour of Human βB1-Crystallin and its Truncated Forms

Bateman

Lubsen

Slingsby

2001

Experimental Eye Research

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“…The expression patterns of the family of ␥-crystallins appear to be correlated with the formation of the decreasing refractive index gradient from the center to the cortex of the adult lens (4,10). The propensity of certain ␥-crystallins to easily form a concentrated phase (11), such as the high T c ␥-crystallins that are enriched in the core region of the lens, probably reflects their "attractive" interactions (12).…”

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confidence: 99%

The X-ray Crystal Structure of Human γS-crystallin C-terminal Domain

Purkiss¹,

Bateman²,

Goodfellow³

et al. 2002

Journal of Biological Chemistry

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␥S-crystallin is a major human lens protein found in the outer region of the eye lens, where the refractive index is low. Because crystallins are not renewed they acquire post-translational modifications that may perturb stability and solubility. In common with other members of the ␤␥-crystallin superfamily, ␥S-crystallin comprises two similar ␤-sheet domains. The crystal structure of the C-terminal domain of human ␥S-crystallin has been solved at 2.4 Å resolution. The structure shows that in the in vitro expressed protein, the buried cysteines remain reduced. The backbone conformation of the "tyrosine corner" differs from that of other ␤␥-crystallins because of deviation from the consensus sequence. The two C-terminal domains in the asymmetric unit are organized about a slightly distorted 2-fold axis to form a dimer with similar geometry to full-length two-domain family members. Two glutamines found in lattice contacts may be important for short range interactions in the lens. An asparagine known to be deamidated in human cataract is located in a highly ordered structural region.

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X-ray diffraction and structure of crystallins

Cited by 39 publications

References 101 publications

Ca2+-binding Motif of βγ-Crystallins

Ca2+-binding Motif of βγ-Crystallins

Association Behaviour of Human βB1-Crystallin and its Truncated Forms

The X-ray Crystal Structure of Human γS-crystallin C-terminal Domain

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