We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1qx2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qx2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qx2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qx2| PDB=1qx2 | SCENE= }}
{{STRUCTURE_1qx2| PDB=1qx2 | SCENE= }}
-
'''X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution'''
+
===X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution===
-
==Overview==
+
<!--
-
The extent of conformational change that calcium binding induces in EF-hand proteins is a key biochemical property specifying Ca(2+) sensor versus signal modulator function. To understand how differences in amino acid sequence lead to differences in the response to Ca(2+) binding, comparative analyses of sequence and structures, combined with model building, were used to develop hypotheses about which amino acid residues control Ca(2+)-induced conformational changes. These results were used to generate a first design of calbindomodulin (CBM-1), a calbindin D(9k) re-engineered with 15 mutations to respond to Ca(2+) binding with a conformational change similar to that of calmodulin. The gene for CBM-1 was synthesized, and the protein was expressed and purified. Remarkably, this protein did not exhibit any non-native-like molten globule properties despite the large number of mutations and the nonconservative nature of some of them. Ca(2+)-induced changes in CD intensity and in the binding of the hydrophobic probe, ANS, implied that CBM-1 does undergo Ca(2+) sensorlike conformational changes. The X-ray crystal structure of Ca(2+)-CBM-1 determined at 1.44 A resolution reveals the anticipated increase in hydrophobic surface area relative to the wild-type protein. A nascent calmodulin-like hydrophobic docking surface was also found, though it is occluded by the inter-EF-hand loop. The results from this first calbindomodulin design are discussed in terms of progress toward understanding the relationships between amino acid sequence, protein structure, and protein function for EF-hand CaBPs, as well as the additional mutations for the next CBM design.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15137763}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15137763 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15137763}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Four-helix domain]]
[[Category: Four-helix domain]]
[[Category: Protein engineering]]
[[Category: Protein engineering]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:48:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:45:30 2008''

Revision as of 00:45, 29 July 2008

Image:1qx2.png

Template:STRUCTURE 1qx2

X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution

Template:ABSTRACT PUBMED 15137763

About this Structure

1QX2 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Designing sequence to control protein function in an EF-hand protein., Bunick CG, Nelson MR, Mangahas S, Hunter MJ, Sheehan JH, Mizoue LS, Bunick GJ, Chazin WJ, J Am Chem Soc. 2004 May 19;126(19):5990-8. PMID:15137763

Page seeded by OCA on Tue Jul 29 03:45:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qx2"
Personal tools