1vyf: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1vyf.gif|left|200px]]
{{Seed}}
[[Image:1vyf.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vyf|  PDB=1vyf  |  SCENE=  }}  
{{STRUCTURE_1vyf|  PDB=1vyf  |  SCENE=  }}  


'''SCHISTOSOMA MANSONI FATTY ACID BINDING PROTEIN IN COMPLEX WITH OLEIC ACID'''
===SCHISTOSOMA MANSONI FATTY ACID BINDING PROTEIN IN COMPLEX WITH OLEIC ACID===




==Overview==
<!--
Schistosoma mansoni fatty acid binding protein (Sm14) was crystallized with bound oleic acid (OLA) and arachidonic acid (ACD), and their structures were solved at 1.85 and 2.4 A resolution, respectively. Sm14 is a vaccine target for schistosomiasis, the second most prevalent parasitic disease in humans. The parasite is unable to synthesize fatty acids depending on the host for these nutrients. Moreover, arachidonic acid (ACD) is required to synthesize prostaglandins employed by schistosomes to evade the host's immune defenses. In the complex, the hydrocarbon tail of bound OLA assumes two conformations, whereas ACD adopts a unique hairpin-looped structure. ACD establishes more specific interactions with the protein, among which the most important is a pi-cation bond between Arg78 and the double bond at C8. Comparison with homologous fatty acid binding proteins suggests that the binding site of Sm14 is optimized to fit ACD. To test the functional implications of our structural data, the affinity of Sm14 for 1,8-anilinonaphthalenesulfonic acid (ANS) has been measured; moreover the binding constants of six different fatty acids were determined from their ability to displace ANS. OLA and ACD exhibited the highest affinities. To determine the rates of fatty acid binding and dissociation we carried out stopped flow kinetic experiments monitoring displacement by (and of) ANS. The binding rate constant of ligands is controlled by a slow pH dependent conformational change, which we propose to have physiological relevance.
The line below this paragraph, {{ABSTRACT_PUBMED_15476393}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15476393 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15476393}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Fatty acid binding protein]]
[[Category: Fatty acid binding protein]]
[[Category: Transport protein]]
[[Category: Transport protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:54:51 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:44:57 2008''

Revision as of 13:44, 27 July 2008

File:1vyf.png

Template:STRUCTURE 1vyf

SCHISTOSOMA MANSONI FATTY ACID BINDING PROTEIN IN COMPLEX WITH OLEIC ACID

Template:ABSTRACT PUBMED 15476393

About this Structure

1VYF is a Single protein structure of sequence from Schistosoma mansoni. Full crystallographic information is available from OCA.

Reference

Schistosoma mansoni fatty acid binding protein: specificity and functional control as revealed by crystallographic structure., Angelucci F, Johnson KA, Baiocco P, Miele AE, Brunori M, Valle C, Vigorosi F, Troiani AR, Liberti P, Cioli D, Klinkert MQ, Bellelli A, Biochemistry. 2004 Oct 19;43(41):13000-11. PMID:15476393

Page seeded by OCA on Sun Jul 27 16:44:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1vyf&oldid=656470"