{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kumar P"],"funding":["European Research Council","BrisSynBio","Israel Science Foundation","Biotechnology and Biological Sciences Research Council"],"pagination":["e4789"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10588367"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(11)"],"pubmed_abstract":["α-Helical coiled coils are common tertiary and quaternary elements of protein structure. In coiled coils, two or more α helices wrap around each other to form bundles. This apparently simple structural motif can generate many architectures and topologies. Coiled coil-forming sequences can be predicted from heptad repeats of hydrophobic and polar residues, hpphppp, although this is not always reliable. Alternatively, coiled-coil structures can be identified using the program SOCKET, which finds knobs-into-holes (KIH) packing between side chains of neighboring helices. SOCKET also classifies coiled-coil architecture and topology, thus allowing sequence-to-structure relationships to be garnered. In 2009, we used SOCKET to create a relational database of coiled-coil structures, CC<sup>+</sup> "],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["CC<sup>+</sup> : A searchable database of validated coiled coils in PDB structures and AlphaFold2 models."],"pmcid":["PMC10588367"],"funding_grant_id":["819318","BB/L01386X/1","1452/18","340764","787173","BB/R00661X/1"],"pubmed_authors":["Schweke H","Petrenas R","Levy ED","Woolfson DN","Kumar P","Dawson WM"],"additional_accession":[]},"is_claimable":false,"name":"CC<sup>+</sup> : A searchable database of validated coiled coils in PDB structures and AlphaFold2 models.","description":"α-Helical coiled coils are common tertiary and quaternary elements of protein structure. In coiled coils, two or more α helices wrap around each other to form bundles. This apparently simple structural motif can generate many architectures and topologies. Coiled coil-forming sequences can be predicted from heptad repeats of hydrophobic and polar residues, hpphppp, although this is not always reliable. Alternatively, coiled-coil structures can be identified using the program SOCKET, which finds knobs-into-holes (KIH) packing between side chains of neighboring helices. SOCKET also classifies coiled-coil architecture and topology, thus allowing sequence-to-structure relationships to be garnered. In 2009, we used SOCKET to create a relational database of coiled-coil structures, CC<sup>+</sup> ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Nov","modification":"2026-05-28T18:14:07.678Z","creation":"2025-02-19T01:52:56.062Z"},"accession":"S-EPMC10588367","cross_references":{"pubmed":["37768271"],"doi":["10.1002/pro.4789"]}}