We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2hyv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hyv.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2hyv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hyv| PDB=2hyv | SCENE= }}
{{STRUCTURE_2hyv| PDB=2hyv | SCENE= }}
-
'''Human Annexin A2 with heparin hexasaccharide bound'''
+
===Human Annexin A2 with heparin hexasaccharide bound===
-
==Overview==
+
<!--
-
Annexin A2 and heparin bind to one another with high affinity and in a calcium-dependent manner, an interaction that may play a role in mediating fibrinolysis. In this study, three heparin-derived oligosaccharides of different lengths were co-crystallized with annexin A2 to elucidate the structural basis of the interaction. Crystal structures were obtained at high resolution for uncomplexed annexin A2 and three complexes of heparin oligosaccharides bound to annexin A2. The common heparin-binding site is situated at the convex face of domain IV of annexin A2. At this site, annexin A2 binds up to five sugar residues from the nonreducing end of the oligosaccharide. Unlike most heparin-binding consensus patterns, heparin binding at this site does not rely on arrays of basic residues; instead, main-chain and side-chain nitrogen atoms and two calcium ions play important roles in the binding. Especially significant is a novel calcium-binding site that forms upon heparin binding. Two sugar residues of the heparin derivatives provide oxygen ligands for this calcium ion. Comparison of all four structures shows that heparin binding does not elicit a significant conformational change in annexin A2. Finally, surface plasmon resonance measurements were made for binding interactions between annexin A2 and heparin polysaccharide in solution at pH 7.4 or 5.0. The combined data provide a clear basis for the calcium dependence of heparin binding to annexin A2.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16882661}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16882661 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16882661}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Hexasaccharide]]
[[Category: Hexasaccharide]]
[[Category: Membrane-binding protein]]
[[Category: Membrane-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:52:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:50:39 2008''

Revision as of 08:50, 29 July 2008

Image:2hyv.png

Template:STRUCTURE 2hyv

Human Annexin A2 with heparin hexasaccharide bound

Template:ABSTRACT PUBMED 16882661

About this Structure

2HYV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of calcium-dependent heparin binding to annexin A2., Shao C, Zhang F, Kemp MM, Linhardt RJ, Waisman DM, Head JF, Seaton BA, J Biol Chem. 2006 Oct 20;281(42):31689-95. Epub 2006 Aug 1. PMID:16882661

Page seeded by OCA on Tue Jul 29 11:50:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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