1bc0: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:1bc0.jpg|left|200px]]
{{Seed}}
[[Image:1bc0.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bc0|  PDB=1bc0  |  SCENE=  }}  
{{STRUCTURE_1bc0|  PDB=1bc0  |  SCENE=  }}  


'''RECOMBINANT RAT ANNEXIN V, W185A MUTANT'''
===RECOMBINANT RAT ANNEXIN V, W185A MUTANT===




==Overview==
<!--  
Annexin V belongs to a family of eukaryotic calcium-dependent membrane-binding proteins. The calcium-binding sites at the annexin-membrane interface have been investigated in some detail; however, little is known about the functional roles of highly conserved interfacial residues that do not coordinate calcium themselves. In the present study, the importance of tryptophan 185, and threonine or serine at positions 72, 144, 228, and 303, in rat annexin V is investigated by site-directed mutagenesis, X-ray crystallography, and functional assays. The high-resolution crystal structures of the mutants show that the mutations do not cause structural perturbations of the annexin molecule itself or disappearance of bound calcium ions from calcium-binding sites. The assays indicate that relative to wild-type annexin V, loss of the methyl substituent at position 72 (Thr72--&gt;Ser) has no effect while loss of the hydroxyl group (Thr72--&gt;Ala or Thr72--&gt;Lys) causes reduction of membrane binding. Multiple lysine substitutions (e.g., Thr72,Ser144,Ser228,Ser303--&gt;Lys) have a greater adverse effect than the single lysine mutation, suggesting that in annexin V the introduction of potentially favorable electrostatic interactions between the lysine side chains and the net negatively charged membrane surface is not sufficient to overcome the loss of the hydroxyl side chains. Replacement of the unique tryptophan, Trp185, by alanine similarly decreases membrane binding affinity. Taken together, the data suggest that the side chains mutated in this study contribute to phospholipid binding and participate directly in intermolecular contacts with phospholipid membrane components.
The line below this paragraph, {{ABSTRACT_PUBMED_9609693}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9609693 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9609693}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Calcium binding protein]]
[[Category: Calcium binding protein]]
[[Category: Phospholipid membrane binding protein]]
[[Category: Phospholipid membrane binding protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:19:22 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:47:53 2008''

Revision as of 15:47, 30 June 2008

File:1bc0.png

Template:STRUCTURE 1bc0

RECOMBINANT RAT ANNEXIN V, W185A MUTANT

Template:ABSTRACT PUBMED 9609693

About this Structure

1BC0 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Mutational and crystallographic analyses of interfacial residues in annexin V suggest direct interactions with phospholipid membrane components., Campos B, Mo YD, Mealy TR, Li CW, Swairjo MA, Balch C, Head JF, Retzinger G, Dedman JR, Seaton BA, Biochemistry. 1998 Jun 2;37(22):8004-10. PMID:9609693

Page seeded by OCA on Mon Jun 30 18:47:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1bc0&oldid=576965"