Structural specificity in coiled-coil interactions

Current Opinion in Structural Biology

Volumn 18, Issue 4, 2008, Pages 477-483

  Grigoryan, Gevorg ^a   Keating, Amy E ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CALCULATION; COILED COIL STRUCTURE; EXPERIMENTAL DESIGN; HUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW;

MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEINS;

EID: 49549094267     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2008.04.008     Document Type: Review

References (56)

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42. ••].
43. •], the authors extended their studies to examine a-d′ interactions in two different contexts. Significant differences between energies measured in two environments implicated a role for 'vertical' interactions (here a′-a-a′) in affecting antiparallel coiled-coil stability. These results are supported by studies in a different, longer anti-parallel coiled coil, and by striking differences in the conformational heterogeneity of side chains in energetically preferred versus nonpreferred combinations.
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49. 5 members. All pair-wise mixtures that could be formed among the two selected peptides and all members of the Jun and Fos families were thermodynamically characterized, resulting in 45 melting temperatures. The selected peptides bound their targets strongly, though other combinations also produced stable interactions. The authors propose a weight-based model that performs well for predicting interaction preferences measured in Ref. [46].
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54. ••] was extended to allow for the simultaneous selection of specificity and stability by including competitor peptides in the selections. Two peptides produced in this way, one to bind Fos and the other to bind Jun, were shown to associate with their respective targets stronger than they homodimerized or interacted with each other's targets.
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