1z6c: Difference between revisions

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[[Image:1z6c.gif|left|200px]]
{{Seed}}
[[Image:1z6c.png|left|200px]]


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{{STRUCTURE_1z6c|  PDB=1z6c  |  SCENE=  }}  
{{STRUCTURE_1z6c|  PDB=1z6c  |  SCENE=  }}  


'''Solution structure of an EGF pair (EGF34) from vitamin K-dependent protein S'''
===Solution structure of an EGF pair (EGF34) from vitamin K-dependent protein S===




==Overview==
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Vitamin K-dependent protein S is a cofactor of activated protein C, a serine protease that regulates blood coagulation. Deficiency of protein S can cause venous thrombosis. Protein S has four EGF domains in tandem; domains 2-4 bind calcium with high affinity whereas domains 1-2 mediate interaction with activated protein C. We have now solved the solution structure of the EGF3-4 fragment of protein S. The linker between the two domains is similar to what has been observed in other calcium-binding EGF domains where it provides an extended conformation. Interestingly, a disagreement between NOE and RDC data revealed a conformational heterogeneity within EGF3 due to a hinge-like motion around Glu186 in the Cys-Glu-Cys sequence, the only point in the domain where flexibility is allowed. The dominant, bent conformation of EGF3 in the pair has no precedent among calcium-binding EGF domains. It is characterized by a change in the psi angle of Glu186 from 160 degrees +/- 40 degrees , as seen in ten other EGF domains, to approximately 0 degrees +/- 15 degrees . NOESY data suggest that Tyr193, a residue not conserved in other calcium-binding EGF domains (except in the homologue Gas6), induces the unique fold of EGF3. However, SAXS data, obtained on EGF1-4 and EGF2-4, showed a dominant, extended conformation in these fragments. This may be due to a counterproductive domain-domain interaction between EGF2 and EGF4 if EGF3 is in a bent conformation. We speculate that the ability of EGF3 to adopt different conformations may be of functional significance in protein-protein interactions involving protein S.
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{{ABSTRACT_PUBMED_15952784}}


==About this Structure==
==About this Structure==
1Z6C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6C OCA].  
1Z6C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6C OCA].  


==Reference==
==Reference==
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[[Category: Thulin, E.]]
[[Category: Thulin, E.]]
[[Category: Egf module]]
[[Category: Egf module]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:13:37 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:56:53 2008''

Revision as of 05:56, 29 July 2008

File:1z6c.png

Template:STRUCTURE 1z6c

Solution structure of an EGF pair (EGF34) from vitamin K-dependent protein S

Template:ABSTRACT PUBMED 15952784

About this Structure

1Z6C is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure of the Ca2+-Binding EGF3-4 pair from vitamin K-dependent protein S: identification of an unusual fold in EGF3., Drakenberg T, Ghasriani H, Thulin E, Thamlitz AM, Muranyi A, Annila A, Stenflo J, Biochemistry. 2005 Jun 21;44(24):8782-9. PMID:15952784

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