2pf1: Difference between revisions

Revision as of 09:58, 28 July 2008

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File:2pf1.png

Template:STRUCTURE 2pf1

STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTIONSTRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1856869

About this StructureAbout this Structure

2PF1 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of bovine prothrombin fragment 1 refined at 2.25 A resolution., Seshadri TP, Tulinsky A, Skrzypczak-Jankun E, Park CH, J Mol Biol. 1991 Jul 20;220(2):481-94. PMID:1856869

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-'''STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTION'''
+===STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The structure of bovine prothrombin fragment 1 has been refined at 2.25 A resolution using high resolution measurements made with the synchrotron beam at CHESS. The synchrotron data were collected photographically by oscillation methods (R-merge = 0.08). These were combined with lower order diffractometer data for refinement purposes. The structure was refined using restrained least-squares methods with the program PROLSQ to a crystallographic R-value of 0.175. The structure includes 105 water molecules with occupancies of greater than 0.6. The first 35 residues (Ala1-Leu35) of the N-terminal gamma-carboxy glutamic acid-domain (Ala1-Cys48) of fragment 1 are disordered as are two carbohydrate chains of Mr approximately 5000; the latter two combine to render 40% of the structure disordered. The folding of the kringle of fragment 1 is related to the close intramolecular contact between the inner loop disulfide groups. Half of the conserved sequence of the kringle forms an inner core surrounding these disulfide groups. The remainder of the sequence conservation is associated with the many turns of the main chain. The Pro95 residue of the kringle has a cis conformation and Tyr74 is ordered in fragment 1, although nuclear magnetic resonance studies indicate that the comparable residue of plasminogen kringle 4 has two positions. Surface accessibility calculations indicate that none of the disulfide groups of fragment 1 is accessible to solvent.
+The line below this paragraph, {{ABSTRACT_PUBMED_1856869}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_1856869}}
 ==About this Structure==
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 [[Category: Skrzypczak-Jankun, E.]]
 [[Category: Tulinsky, A.]]
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