1fi6
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1fi6.gif|left|200px]] | [[Image:1fi6.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1fi6", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1fi6| PDB=1fi6 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''SOLUTION STRUCTURE OF THE REPS1 EH DOMAIN''' | '''SOLUTION STRUCTURE OF THE REPS1 EH DOMAIN''' | ||
| Line 27: | Line 24: | ||
[[Category: Baleja, J D.]] | [[Category: Baleja, J D.]] | ||
[[Category: Kim, S.]] | [[Category: Kim, S.]] | ||
| - | [[Category: | + | [[Category: Calcium]] |
| - | [[Category: | + | [[Category: Ef hand]] |
| - | [[Category: | + | [[Category: Eps15 homology domain]] |
| - | [[Category: | + | [[Category: Ras signal transduction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:21:22 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:21, 2 May 2008
SOLUTION STRUCTURE OF THE REPS1 EH DOMAIN
Overview
The recently described EH domain recognizes proteins containing Asn-Pro-Phe (NPF) sequences. Using nuclear magnetic resonance (NMR) data, we determined the solution structure of the EH domain from the Reps1 protein and characterized its binding to linear and cyclic peptides derived from a novel targeting protein. The structure calculation included 1143 distance restraints and 122 angle restraints and resulted in structures with a root-mean-square deviation of 0.40 +/- 0.05 A for backbone atoms of superimposed secondary structural elements. The structure comprises two helix-loop-helix motifs characteristic of EF-hand domains. Titration data with NPF-containing peptides showed evidence of intermediate exchange on the NMR chemical shift time scale, which required an analysis that includes curve fitting to obtain accurate equilibrium constants and dissociation rate constants. The cyclic and linear peptides bound with similar affinities (Kd = 65 +/- 17 and 46 +/- 14 microM, respectively) and to the same hydrophobic pocket formed between helices B and C. The cyclic peptide formed a complex that dissociated more slowly (k(off) = 440 +/- 110 s(-1)) than the linear peptide (k(off) = 1800 +/- 250 s(-1)), but had little change in affinity because of the slower rate of association of the cyclic peptide. In addition, we characterized binding to a peptide containing a DPF sequence (Kd = 0.5 +/- 0.2 mM). The characterization of binding between the Reps1 EH domain and its target proteins provides information about their role in endocytosis.
About this Structure
1FI6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences., Kim S, Cullis DN, Feig LA, Baleja JD, Biochemistry. 2001 Jun 12;40(23):6776-85. PMID:11389591 Page seeded by OCA on Fri May 2 16:21:22 2008
