NDLI: Resonance assignments for latherin, a natural surfactant protein from horse sweat

Content Provider	PubMed Central
Author	Vance, Steven J. Mcdonald, Rhona E. Cooper, Alan Kennedy, Malcolm W. Smith, Brian O.
Abstract	Latherin is an intrinsically surfactant protein of ~23 kDa found in the sweat and saliva of horses. Its function is probably to enhance the translocation of sweat water from the skin to the surface of the pelt for evaporative cooling. Its role in saliva may be to enhance the wetting, softening and maceration of the dry, fibrous food for which equines are adapted. Latherin is unusual in its relatively high content of aliphatic amino acids (~25 % leucines) that might contribute to its surfactant properties. Latherin is related to the palate, lung, and nasal epithelium carcinoma-associated proteins (PLUNCs) of mammals, at least one of which is now known to exhibit similar surfactant activity to latherin. No structures of any PLUNC protein are currently available. 15N,13C-labelled recombinant latherin was produced in Escherichia coli, and essentially all of the resonances were assigned despite the signal overlap due to the preponderance of leucines. The most notable exceptions include a number of residues located in an apparently dynamic loop region between residues 145 and 154. The assignments have been deposited with BMRB accession number 19067.
Related Links	http://dx.doi.org/10.1007/s12104-013-9485-3
Ending Page	216
Page Count	4
Starting Page	213
File Format	PDF
ISSN	18742718
e-ISSN	1874270X
Journal	Biomolecular Nmr Assignments
Issue Number	1
Volume Number	8
Language	English
Publisher	Springer Netherlands
Publisher Date	2014-04-01
Access Restriction	Open
Rights Holder	Springer Netherlands
Subject Keyword	Biochemistry Structural Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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