1n41: Difference between revisions

Revision as of 10:05, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n41.png

Template:STRUCTURE 1n41

Crystal Structure of Annexin V K27E MutantCrystal Structure of Annexin V K27E Mutant

Template:ABSTRACT PUBMED 12401794

About this StructureAbout this Structure

1N41 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 10:05:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1n41.gif|left|200px]]
+{{Seed}}
+[[Image:1n41.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1n41|  PDB=1n41  |  SCENE=  }}
-'''Crystal Structure of Annexin V K27E Mutant'''
+===Crystal Structure of Annexin V K27E Mutant===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12401794}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12401794 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12401794}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Calcium]]
 [[Category: Phospholipid membrane binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:03:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:05:42 2008''