1fry
From Proteopedia
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'''THE SOLUTION STRUCTURE OF SHEEP MYELOID ANTIMICROBIAL PEPTIDE, RESIDUES 1-29 (SMAP29)''' | '''THE SOLUTION STRUCTURE OF SHEEP MYELOID ANTIMICROBIAL PEPTIDE, RESIDUES 1-29 (SMAP29)''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FRY is a [[Single protein]] structure | + | 1FRY is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Waring, A J.]] | [[Category: Waring, A J.]] | ||
[[Category: Wu, H.]] | [[Category: Wu, H.]] | ||
| - | [[Category: | + | [[Category: Random-ordered coil-loop]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:41:35 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:41, 2 May 2008
THE SOLUTION STRUCTURE OF SHEEP MYELOID ANTIMICROBIAL PEPTIDE, RESIDUES 1-29 (SMAP29)
Overview
The CD spectra of SMAP-29, an antimicrobial peptide from sheep, showed disordered structure in aqueous buffers, and significant helicity in membrane-like environments, including SDS micelles, lipopolysaccharide (LPS) dispersions, and trifluoroethanol buffer systems. A structure determined by NMR in 40% perdeuterated trifluoroethanol indicated that residues 8-17 were helical, residues 18-19 formed a hinge, and residues 20-28 formed an ordered, hydrophobic segment. SMAP-29 was flexible in 40% trifluoroethanol, forming two sets of conformers that differed in the relative orientation of the N-terminal domain. We used a chromogenic Limulus assay to determine the EC50 of the peptide (the concentration that bound 50% of the added LPS). Studies with full-length and truncated SMAP-29 molecules revealed that each end of the holopeptide contained an LPS-binding domain. The higher affinity LPS-binding domain was situated in the flexible N-terminal portion. LPS binding to full-length SMAP-29 showed positive cooperativity, so the EC50 of the peptide (2.6 microm) was considerably lower than that of the individual LPS-binding domains. LPS-binding studies with a mixture of truncated peptides revealed that this cooperativity was primarily intramolecular (i.e. involving the N- and C-terminal LPS-binding sites of the same peptide molecule). CAP-18[106 -142], an antimicrobial cathelicidin peptide of rabbits, resembled SMAP-29 in that it contained N- and C-terminal LPS-binding domains, had an EC50 of 2.5 microm, and bound LPS with positive cooperativity. We conclude that the presence of multiple binding sites that function cooperatively allow peptides such as SMAP-29 and CAP-18 to bind LPS with high affinity.
About this Structure
1FRY is a Single protein structure. Full crystallographic information is available from OCA.
Reference
SMAP-29 has two LPS-binding sites and a central hinge., Tack BF, Sawai MV, Kearney WR, Robertson AD, Sherman MA, Wang W, Hong T, Boo LM, Wu H, Waring AJ, Lehrer RI, Eur J Biochem. 2002 Feb;269(4):1181-9. PMID:11856344 Page seeded by OCA on Fri May 2 16:41:35 2008
