<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kumar P</submitter><funding>European Research Council</funding><funding>BrisSynBio</funding><funding>Israel Science Foundation</funding><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>e4789</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10588367</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>32(11)</volume><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&lt;sup>+&lt;/sup> </pubmed_abstract><journal>Protein science : a publication of the Protein Society</journal><pubmed_title>CC&lt;sup>+&lt;/sup> : A searchable database of validated coiled coils in PDB structures and AlphaFold2 models.</pubmed_title><pmcid>PMC10588367</pmcid><funding_grant_id>819318</funding_grant_id><funding_grant_id>BB/L01386X/1</funding_grant_id><funding_grant_id>1452/18</funding_grant_id><funding_grant_id>340764</funding_grant_id><funding_grant_id>787173</funding_grant_id><funding_grant_id>BB/R00661X/1</funding_grant_id><pubmed_authors>Schweke H</pubmed_authors><pubmed_authors>Petrenas R</pubmed_authors><pubmed_authors>Levy ED</pubmed_authors><pubmed_authors>Woolfson DN</pubmed_authors><pubmed_authors>Kumar P</pubmed_authors><pubmed_authors>Dawson WM</pubmed_authors></additional><is_claimable>false</is_claimable><name>CC&lt;sup>+&lt;/sup> : A searchable database of validated coiled coils in PDB structures and AlphaFold2 models.</name><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&lt;sup>+&lt;/sup> </description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Nov</publication><modification>2026-05-28T18:14:07.678Z</modification><creation>2025-02-19T01:52:56.062Z</creation></dates><accession>S-EPMC10588367</accession><cross_references><pubmed>37768271</pubmed><doi>10.1002/pro.4789</doi></cross_references></HashMap>