1re4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1re4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1re4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1re4| PDB=1re4 | SCENE= }}
{{STRUCTURE_1re4| PDB=1re4 | SCENE= }}
-
'''Crystal Structure of Fragment D of BbetaD398A Fibrinogen'''
+
===Crystal Structure of Fragment D of BbetaD398A Fibrinogen===
-
==Overview==
+
<!--
-
We synthesized three fibrinogen variants, BbetaE397A, BbetaD398A, and BbetaD432A, with substitutions at positions identified in crystallographic studies as critical for binding the "B" peptide, Gly-His-Arg-Pro-amide (GHRPam), to the "b" polymerization site. We examined thrombin- and batroxobin-catalyzed polymerization by turbidity measurements and found that BbetaE397A and BbetaD398A were impaired while BbetaD432A was normal. Changes in polymerization as a function of calcium were similar for variant and normal fibrinogens. We determined crystal structures of fragment D from the variant BbetaD398A in the absence and presence of GHRPam. In the absence of peptide, the structure showed that the alanine substitution altered only specific local interactions, as alignment of the variant structure with the analogous normal structure resulted in an RMSD of 0.53 A over all atoms. The structure also showed reduced occupancy of the beta2 calcium-binding site that includes the side chain carbonyl of BbetaD398, suggesting that calcium was not bound at this site in our polymerization studies. In the presence of peptide, the structure showed that GHRPam was not bound in the "b" site and the conformational changes associated with peptide binding to normal fragment D did not occur. This structure also showed GHRPam bound in the "a" polymerization site, although in two different conformations. Calcium binding was associated with only one of these conformations, suggesting that calcium binding to the gamma2-site and an alternative peptide conformation were induced by crystal packing. We conclude that BbetaE397 and BbetaD398 are essential for the "B:b" interaction, while BbetaD432 is not.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14992584}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14992584 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14992584}}
==Disease==
==Disease==
Line 34: Line 38:
[[Category: Recombinant fibrinogen fragment d]]
[[Category: Recombinant fibrinogen fragment d]]
[[Category: Variant fibrinogen]]
[[Category: Variant fibrinogen]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:23:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:36:58 2008''

Revision as of 09:36, 29 July 2008

Image:1re4.png

Template:STRUCTURE 1re4

Contents

Crystal Structure of Fragment D of BbetaD398A Fibrinogen

Template:ABSTRACT PUBMED 14992584

Disease

Known disease associated with this structure: Afibrinogenemia, congenital OMIM:[134820], Amyloidosis, hereditary renal OMIM:[134820], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[134820], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[134820], Afibrinogenemia, congenital OMIM:[134830], Dysfibrinogenemia, beta type OMIM:[134830], Thrombophilia, dysfibrinogenemic OMIM:[134830], Dysfibrinogenemia, gamma type OMIM:[134850], Hypofibrinogenemia, gamma type OMIM:[134850], Thrombophilia, dysfibrinogenemic OMIM:[134850]

About this Structure

1RE4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

B beta Glu397 and B beta Asp398 but not B beta Asp432 are required for "B:b" interactions., Kostelansky MS, Bolliger-Stucki B, Betts L, Gorkun OV, Lord ST, Biochemistry. 2004 Mar 9;43(9):2465-74. PMID:14992584

Page seeded by OCA on Tue Jul 29 12:36:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1re4"
Personal tools