Domain closure in lactoferrin : two hinges produce a see-saw motion between alternative close-packed interfaces
In: Journal of molecular biology, Jg. 234 (1993), Heft 2, S. 357-372
academicJournal
- print, 1 p. 1/2
Zugriff:
Lactoferrin is an iron transport protein. Upon binding iron, the two domains in the N-terminal half of the molecule move together. Previous work has shown that this domain closure involves two hinges. Using the newly refined structure of the open form, the structural mechanism underlying this motion is analyzed here in detail. Upon closure the domains rotate 54° essentially as rigid bodies. The axis of rotation passes through the two β-strands linking the domains. These strands contain hinges in the sense that three large torsion angle changes are responsible for the bulk of the motion while smaller torsion angle changes in neighboring residues are responsible for the remainder of the motion.
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Domain closure in lactoferrin : two hinges produce a see-saw motion between alternative close-packed interfaces
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Autor/in / Beteiligte Person: | GERSTEIN, M ; ANDERSON, B. F ; NORRIS, G. E ; BAKER, E. N ; LESK, A. M ; CHOTHIA, C |
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Zeitschrift: | Journal of molecular biology, Jg. 234 (1993), Heft 2, S. 357-372 |
Veröffentlichung: | Oxford: Elsevier, 1993 |
Medientyp: | academicJournal |
Umfang: | print, 1 p. 1/2 |
ISSN: | 0022-2836 (print) |
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