2baf
From Proteopedia
(New page: 200px<br /><applet load="2baf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2baf" /> '''Bovine Fibrinogen alpha-C Domain'''<br /> =...) |
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| - | [[Image:2baf.gif|left|200px]]<br /><applet load="2baf" size=" | + | [[Image:2baf.gif|left|200px]]<br /><applet load="2baf" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Bovine Fibrinogen alpha-C Domain'''<br /> | '''Bovine Fibrinogen alpha-C Domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The NMR solution structure of the bovine fibrinogen alphaC-domain | + | The NMR solution structure of the bovine fibrinogen alphaC-domain fragment, including residues Aalpha374-538, reveals a type-I' beta-hairpin, restricted at the base by a C423-C453 disulfide linkage and a short turn preceding C423. Although both faces of the hairpin are formed mainly by hydrophilic residues, one of them is uncharged while the other has a characteristic pattern of charged residues which are highly conserved among vertebrate species. Chemical shift indexing and relaxation data indicate the presence of a collapsed hydrophobic region next to the hairpin that includes approximately 30 residues with slower concerted motion and higher content of nonpolar residues and, according to a previous study (Tsurupa, G., Tsonev, L., and Medved, L. (2002) Biochemistry 41, 6449-6459), may cooperate with the hairpin to form a compact cooperative unit (domain). Structure and relaxation data show that the region between C423 and C453 is populated by both random coil and beta-structure, suggesting that the cooperative structure in the isolated alphaC-domain is intrinsically unstable. This observation is in agreement with a very low energy of stabilization of the Aalpha374-538 fragment determined in unfolding experiments. The low stability of the alphaC-domain suggests a possible explanation for the previously observed intra- and intermolecular interactions of these domains in fibrinogen and fibrin. |
==About this Structure== | ==About this Structure== | ||
| - | 2BAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 2BAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burton, R | + | [[Category: Burton, R A.]] |
[[Category: beta hairpin]] | [[Category: beta hairpin]] | ||
[[Category: fibrinogen]] | [[Category: fibrinogen]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:43 2008'' |
Revision as of 14:35, 21 February 2008
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Bovine Fibrinogen alpha-C Domain
Overview
The NMR solution structure of the bovine fibrinogen alphaC-domain fragment, including residues Aalpha374-538, reveals a type-I' beta-hairpin, restricted at the base by a C423-C453 disulfide linkage and a short turn preceding C423. Although both faces of the hairpin are formed mainly by hydrophilic residues, one of them is uncharged while the other has a characteristic pattern of charged residues which are highly conserved among vertebrate species. Chemical shift indexing and relaxation data indicate the presence of a collapsed hydrophobic region next to the hairpin that includes approximately 30 residues with slower concerted motion and higher content of nonpolar residues and, according to a previous study (Tsurupa, G., Tsonev, L., and Medved, L. (2002) Biochemistry 41, 6449-6459), may cooperate with the hairpin to form a compact cooperative unit (domain). Structure and relaxation data show that the region between C423 and C453 is populated by both random coil and beta-structure, suggesting that the cooperative structure in the isolated alphaC-domain is intrinsically unstable. This observation is in agreement with a very low energy of stabilization of the Aalpha374-538 fragment determined in unfolding experiments. The low stability of the alphaC-domain suggests a possible explanation for the previously observed intra- and intermolecular interactions of these domains in fibrinogen and fibrin.
About this Structure
2BAF is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR., Burton RA, Tsurupa G, Medved L, Tjandra N, Biochemistry. 2006 Feb 21;45(7):2257-66. PMID:16475814
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