1n42: Difference between revisions

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[[Image:1n42.gif|left|200px]]
{{Seed}}
[[Image:1n42.png|left|200px]]


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{{STRUCTURE_1n42|  PDB=1n42  |  SCENE=  }}  
{{STRUCTURE_1n42|  PDB=1n42  |  SCENE=  }}  


'''Crystal Structure of Annexin V R149E Mutant'''
===Crystal Structure of Annexin V R149E Mutant===




==Overview==
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Annexin V is an abundant eukaryotic protein that binds phospholipid membranes in a Ca(2+)-dependent manner. In the present studies, site-directed mutagenesis was combined with x-ray crystallography and solution liposome binding assays to probe the functional role of a cluster of interfacial basic residues in annexin V. Four mutants were investigated: R23E, K27E, R61E, and R149E. All four mutants exhibited a significant reduction in adsorption to phospholipid membranes relative to the wild-type protein, and the R23E mutation was the most deleterious. Crystal structures of wild-type and mutant proteins were similar except for local changes in salt bridges involving basic cluster residues. The combined data indicate that Arg(23) is a major determinant for interfacial phospholipid binding and participates in an intermolecular salt bridge that is key for trimer formation on the membrane surface. Together, crystallographic and solution data provide evidence that the interfacial basic cluster is a locus where trimerization is synergistically coupled to membrane phospholipid binding.
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{{ABSTRACT_PUBMED_12401794}}


==About this Structure==
==About this Structure==
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[[Category: Membrane binding protein]]
[[Category: Membrane binding protein]]
[[Category: Phospholipid]]
[[Category: Phospholipid]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:03:56 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:32:41 2008''

Revision as of 02:32, 29 July 2008

File:1n42.png

Template:STRUCTURE 1n42

Crystal Structure of Annexin V R149E Mutant

Template:ABSTRACT PUBMED 12401794

About this Structure

1N42 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces., Mo Y, Campos B, Mealy TR, Commodore L, Head JF, Dedman JR, Seaton BA, J Biol Chem. 2003 Jan 24;278(4):2437-43. Epub 2002 Oct 24. PMID:12401794

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