5hfy

From Proteopedia

Backbone Modifications in the Protein GB1 Helix: beta-2-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35

Structural highlights

5hfy is a 2 chain structure with sequence from Streptococcus sp. 'group G'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.95Å
Ligands:	62H, B3K, B3X, NH2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SPG2_STRSG

Publication Abstract from PubMed

We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an alpha-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in alpha-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences.

Comparison of design strategies for alpha-helix backbone modification in a protein tertiary fold.,Tavenor NA, Reinert ZE, Lengyel GA, Griffith BD, Horne WS Chem Commun (Camb). 2016 Feb 25;52(19):3789-92. doi: 10.1039/c6cc00273k. PMID:26853882^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations

3 reviews cite this structure

Systematic Targeting of Protein-Protein Interactions.

Modell et al. (2016)

2 more

14 other articles

No citations found

References

↑ Tavenor NA, Reinert ZE, Lengyel GA, Griffith BD, Horne WS. Comparison of design strategies for alpha-helix backbone modification in a protein tertiary fold. Chem Commun (Camb). 2016 Feb 25;52(19):3789-92. doi: 10.1039/c6cc00273k. PMID:26853882 doi:http://dx.doi.org/10.1039/c6cc00273k

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

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PDB ID 5hfy

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5hfy

From Proteopedia

Backbone Modifications in the Protein GB1 Helix: beta-2-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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