| http://purl.uniprot.org/citations/15520380 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15520380 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15520380 | http://www.w3.org/2000/01/rdf-schema#comment | "Coiled-coil motifs are ubiquitous mediators of specific protein-protein interactions through the formation of interlocking hydrophobic seams between alpha-helical chains. Residues that form these seams occur at the first (a) and fourth (d) positions of a characteristic 7-aa repeat and are primarily aliphatic. The potential of aromatic residues to promote helix association in a coiled coil was explored by engineering a "Trp-zipper" protein with Trp residues at all 14 a and d positions. The protein forms a discrete, stable, alpha-helical pentamer in water at physiological pH. Its 1.45-A crystal structure reveals a parallel, five-stranded coiled coil, a previously uncharacterized type of "knobs-into-holes" packing interaction between interfacial Trp side chains, and an unusual approximately 8-A-diameter axial channel lined with indole rings that is filled with polyethylene glycol 400 and water and sulfate ion molecules. The engineered Trp-zipper pentamer enlarges current views of coiled-coil assembly, molecular recognition, and protein engineering, and may serve as a soluble model for membrane ion channels."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0405319101"xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0405319101"xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Deng Y."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Deng Y."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Lu M."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Lu M."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Kallenbach N.R."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Kallenbach N.R."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Yong W."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/author | "Yong W."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/pages | "16156-16161"xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/pages | "16156-16161"xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/title | "Atomic structure of a tryptophan-zipper pentamer."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/title | "Atomic structure of a tryptophan-zipper pentamer."xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/volume | "101"xsd:string |
| http://purl.uniprot.org/citations/15520380 | http://purl.uniprot.org/core/volume | "101"xsd:string |