Computer-generated model of the quaternary structure of alpha crystallin in the lens

Groth-Vasselli, Barbara; Kumosinski, Thomas F.; Farnsworth, Patricia N.

doi:10.1016/s0014-4835(05)80044-2

Cited by 46 publications

(12 citation statements)

References 22 publications

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“…Both experimental data [16] and our model of the quaternary structure [8] show that the radius of ~-crystallin aggregate (4042 eta subunits) is ~ 100/~ and volume occupied by the subunits is only ~ 30%. This provides sufficient space to accommodate binding of y-crystallin and other proteins.…”

Section: Resultsmentioning

confidence: 71%

“…Consequently, the tertiary structure of the two subunits of ~-crystallin [7] and the quaternary structure of its aggregate [8] have been proposed by our group using computer assisted molecular modeling in conjunction with experimental data on the secondary structure. The validity of these working models can be tested by how well they correlate with experimental data accumulated over the past several decades.…”

Section: Introductionmentioning

confidence: 99%

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α‐Crystallin quaternary structure: molecular basis for its chaperone activity

et al. 1995

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Key wordY: c~-Crystallin; Chaperone; y-Crystallin; Lens y-B crystallin (formerly y-II) [9] are used to explain, on the molecular level, recent experimental observations [10,11]. The data show that c~-crystallin binds to partially heat denatured soluble 7/-crystallin in a 1 : I monomer stoichiometry. This binding protects y-crystallin from further heat induced thermal denaturation [10] as well as thiol oxidation [11]. Wang and Spector [10] suggest that each monomer in ~-crystallin binds a soluble, partially denatured y-crystallin molecule at a single binding site. The 1 : 1 ratio has also been reported by Borkman et al. [12] for the ~/y complex following UV radiation. Using our quaternary model for simulation of these observations, the results show that y-crystallin N-terminal domain is intercalated in the space between the adjacent C-terminal domains of ~-crystallin subunits.

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Section: Resultsmentioning

confidence: 71%

Section: Introductionmentioning

confidence: 99%

α‐Crystallin quaternary structure: molecular basis for its chaperone activity

et al. 1995

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“…Mammalian sHsps such as αA‐ and αB‐crystallin and Hsp27 are highly dynamic and comprised of a variable number of subunits, properties which contribute to the polydisperse nature of the assemblies and thwart attempts at crystallization. The quaternary structure of α‐crystallin is, therefore, a highly topical issue and many discrepant theoretical models have been proposed 13–17…”

Section: Introductionmentioning

confidence: 99%

Virtual microscopy for cytology proficiency testing: Are we there yet?

Stewart

Miyazaki²,

Bevans‐Wilkins

et al. 2007

Cancer

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The current results confirmed the feasibility of VM for proficiency tests with 2 main problems noted. First, primary screeners had difficulties meeting the mandatory time allocation; however, with increased familiarity with the software, the screening times decreased. Second, the 3-dimensional nature of certain lesions made them difficult to interpret even on monolayered, liquid-based preparations. Creation of a more user-friendly software interface and better methods to capture depth of focus should make this a valid measure of cervicovaginal cytopathologic interpretive competence.

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“…Greater surface area exposure is expected to enhance chaperone‐like activity. A proposed ‘open’ micellar structure of α‐crystallin quaternary structure [18,30,31] is devoid of dimers and tetramers. Therefore, it represents maximum surface exposure.…”

Section: Discussionmentioning

confidence: 99%

Self‐complementary motifs (SCM) in α‐crystallin small heat shock proteins

Farnsworth

Singh

2000

FEBS Letters

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Small heat shock proteins (sHsp) have been implicated in many cell processes involving the dynamics of proteinp rotein interactions. Two unusual sequences containing selfcomplementary motifs (SCM) have been identified within the conserved K K-crystallin domain of sHsps. When two SCMs are aligned in an anti-parallel direction (N to C and C to N), the charged or polar residues form either salt bridges or hydrogen bonds while the non-polar residues participate in hydrophobic interactions. When aligned in reverse order, the residues of these motifs in K K-crystallin subunits form either hydrophobic and/or polar interactions. Homology based molecular modeling of the C-terminal domain of K K-crystallin subunits using the crystal structure of MjHSP16.5 suggests that SCM1 and 2 participate in stabilizing secondary structure and subunit interactions. Also there is overwhelming evidence that these motifs are important in the chaperone-like activity of K K-crystallin subunits. These sequences are conserved and appear to be characteristic of the entire sHsp superfamily. Similar motifs are also present in the Hsp70 family and the immunoglobulin superfamily. ß

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Computer-generated model of the quaternary structure of alpha crystallin in the lens

Cited by 46 publications

References 22 publications

α‐Crystallin quaternary structure: molecular basis for its chaperone activity

α‐Crystallin quaternary structure: molecular basis for its chaperone activity

Virtual microscopy for cytology proficiency testing: Are we there yet?

Self‐complementary motifs (SCM) in α‐crystallin small heat shock proteins

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