This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2pf1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pf1.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pf1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pf1| PDB=2pf1 | SCENE= }}
{{STRUCTURE_2pf1| PDB=2pf1 | SCENE= }}
-
'''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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1856869 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1856869}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Skrzypczak-Jankun, E.]]
[[Category: Skrzypczak-Jankun, E.]]
[[Category: Tulinsky, A.]]
[[Category: Tulinsky, A.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:59:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:58:29 2008''

Revision as of 06:58, 28 July 2008

Image:2pf1.png

Template:STRUCTURE 2pf1

STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1856869

About this Structure

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

Reference

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

Page seeded by OCA on Mon Jul 28 09:58:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pf1"
Personal tools