2gbm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="2gbm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gbm, resolution 1.55&Aring;" /> '''Crystal Structure o...)
Line 1: Line 1:
-
[[Image:2gbm.gif|left|200px]]<br />
+
[[Image:2gbm.gif|left|200px]]<br /><applet load="2gbm" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="2gbm" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="2gbm, resolution 1.55&Aring;" />
caption="2gbm, resolution 1.55&Aring;" />
'''Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin'''<br />
'''Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin'''<br />
==Overview==
==Overview==
-
We previously concluded that, judging from NMR chemical shifts, the, effects of insertions into ubiquitin on its conformation appear to depend, primarily on the site of insertion rather than the sequence of the, insertion. To obtain a more complete and atomic-resolution understanding, of how these insertions modulate the conformation of ubiquitin, we have, solved the crystal structures of four insertional mutants of ubiquitin., Insertions between residues 9 and 10 of ubiquitin are minimally perturbing, to the remainder of the protein, while larger alterations occur when the, insertion is between residues 35 and 36. Further, the alterations in, response to insertions are very similar for each mutant at a given site., Two insertions, one at each site, were designed from structurally, homologous proteins. Interestingly, the secondary structure within these, five to seven amino acid residue insertions is conserved in the new, protein. Overall, the crystal structures support the previous conclusion, that the conformational effects of these insertions are determined largely, by the site of insertion and only secondarily by the sequence of the, insert.
+
We previously concluded that, judging from NMR chemical shifts, the effects of insertions into ubiquitin on its conformation appear to depend primarily on the site of insertion rather than the sequence of the insertion. To obtain a more complete and atomic-resolution understanding of how these insertions modulate the conformation of ubiquitin, we have solved the crystal structures of four insertional mutants of ubiquitin. Insertions between residues 9 and 10 of ubiquitin are minimally perturbing to the remainder of the protein, while larger alterations occur when the insertion is between residues 35 and 36. Further, the alterations in response to insertions are very similar for each mutant at a given site. Two insertions, one at each site, were designed from structurally homologous proteins. Interestingly, the secondary structure within these five to seven amino acid residue insertions is conserved in the new protein. Overall, the crystal structures support the previous conclusion that the conformational effects of these insertions are determined largely by the site of insertion and only secondarily by the sequence of the insert.
 +
 
 +
==Disease==
 +
Known disease associated with this structure: Cleft palate, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191339 191339]]
==About this Structure==
==About this Structure==
-
2GBM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ARS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GBM OCA].
+
2GBM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ARS:'>ARS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GBM OCA].
==Reference==
==Reference==
Line 14: Line 16:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Ferraro, D.J.]]
+
[[Category: Ferraro, D J.]]
-
[[Category: Ferraro, D.M.]]
+
[[Category: Ferraro, D M.]]
[[Category: Ramaswamy, S.]]
[[Category: Ramaswamy, S.]]
-
[[Category: Robertson, A.D.]]
+
[[Category: Robertson, A D.]]
[[Category: ARS]]
[[Category: ARS]]
[[Category: loop insertion]]
[[Category: loop insertion]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:17:00 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:30:04 2008''

Revision as of 15:30, 21 February 2008


2gbm, resolution 1.55Å

Drag the structure with the mouse to rotate

Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin

Contents

Overview

We previously concluded that, judging from NMR chemical shifts, the effects of insertions into ubiquitin on its conformation appear to depend primarily on the site of insertion rather than the sequence of the insertion. To obtain a more complete and atomic-resolution understanding of how these insertions modulate the conformation of ubiquitin, we have solved the crystal structures of four insertional mutants of ubiquitin. Insertions between residues 9 and 10 of ubiquitin are minimally perturbing to the remainder of the protein, while larger alterations occur when the insertion is between residues 35 and 36. Further, the alterations in response to insertions are very similar for each mutant at a given site. Two insertions, one at each site, were designed from structurally homologous proteins. Interestingly, the secondary structure within these five to seven amino acid residue insertions is conserved in the new protein. Overall, the crystal structures support the previous conclusion that the conformational effects of these insertions are determined largely by the site of insertion and only secondarily by the sequence of the insert.

Disease

Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]

About this Structure

2GBM is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structures of ubiquitin insertion mutants support site-specific reflex response to insertions hypothesis., Ferraro DM, Ferraro DJ, Ramaswamy S, Robertson AD, J Mol Biol. 2006 Jun 2;359(2):390-402. Epub 2006 Apr 5. PMID:16647719

Page seeded by OCA on Thu Feb 21 17:30:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools