Ontology highlight
ABSTRACT:
SUBMITTER: Tuinstra RL
PROVIDER: S-EPMC2278211 | biostudies-literature | 2008 Apr
REPOSITORIES: biostudies-literature
Tuinstra Robbyn L RL Peterson Francis C FC Kutlesa Snjezana S Elgin E Sonay ES Kron Michael A MA Volkman Brian F BF
Proceedings of the National Academy of Sciences of the United States of America 20080325 13
Proteins often have multiple functional states, which might not always be accommodated by a single fold. Lymphotactin (Ltn) adopts two distinct structures in equilibrium, one corresponding to the canonical chemokine fold consisting of a monomeric three-stranded beta-sheet and carboxyl-terminal helix. The second Ltn structure solved by NMR reveals a dimeric all-beta-sheet arrangement with no similarity to other known proteins. In physiological solution conditions, both structures are significantl ...[more]