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1fac

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{{STRUCTURE_1fac| PDB=1fac | SCENE= }}
{{STRUCTURE_1fac| PDB=1fac | SCENE= }}
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'''COAGULATION FACTOR VIII, NMR, 1 STRUCTURE'''
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===COAGULATION FACTOR VIII, NMR, 1 STRUCTURE===
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==Overview==
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A 21 residue peptide from the C2 domain of the antihaemophilic factor VIII competes with factor VIII for membrane-binding sites in vitro. Here, we provide the structure and topography of the peptide in solution, on dodecylphosphocholine (DPC) micelles, determined using 1H-NMR spectroscopy. The peptide assumes an amphipathic structure comprising an extended N-terminal region and a C-terminal helix. The average root-mean-square deviation is 0.7+/-0.2 A for the superimposition of the backbone atoms of Ile6 to Arg18 on the lowest energy structure. Whereas the backbone conformation is similar to that in SDS micelles, the Trp11 side-chain orientation is dramatically changed. The indole ring is nearly parallel to the peptide backbone in SDS micelles but perpendicular in DPC micelles. Further, pKa values of the two histidines change by more than 1 pH unit in SDS relative to DPC, which localizes the imidazole rings to the interfacial region. Line-broadening induced by spin-labelled phosphatidylcholine shows that most of the amino acid side-chains that penetrate the DPC micelle are hydrophobic. Thus, the long axis of the peptide lies parallel to the micelle surface and the hydrophobic face of the alpha-helix provides hydrophobic membrane interaction. The large chemical shift changes shown by Trp11 and N-terminal amino acid residues in SDS relative to DPC indicate that this region may be involved in membrane phospholipid recognition. 1H-NMR assignments, CD spectra, one-dimensional 1H-NMR spectra, chemical-shift analysis and nuclear Overhauser effect information are reported in Supplementary Publication SUP 50184 (11 pages), which has been deposited at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K, from whom copies can be obtained according to the terms indicated in Biochem. J. (1997) 321, 8.
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{{ABSTRACT_PUBMED_9601086}}
==About this Structure==
==About this Structure==
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1FAC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAC OCA].
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1FAC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAC OCA].
==Reference==
==Reference==
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[[Category: Veeraraghavan, S.]]
[[Category: Veeraraghavan, S.]]
[[Category: Coagulation factor]]
[[Category: Coagulation factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:05:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:57:01 2008''

Revision as of 23:57, 30 June 2008

Image:1fac.png

Template:STRUCTURE 1fac

COAGULATION FACTOR VIII, NMR, 1 STRUCTURE

Template:ABSTRACT PUBMED 9601086

About this Structure

1FAC is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Structure and topography of the membrane-binding C2 domain of factor VIII in the presence of dodecylphosphocholine micelles., Veeraraghavan S, Baleja JD, Gilbert GE, Biochem J. 1998 Jun 1;332 ( Pt 2):549-55. PMID:9601086

Page seeded by OCA on Tue Jul 1 02:57:01 2008

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