This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1uo1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1uo1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1uo1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uo1| PDB=1uo1 | SCENE= }}
{{STRUCTURE_1uo1| PDB=1uo1 | SCENE= }}
-
'''STRUCTURE BASED ENGINEERING OF INTERNAL MOLECULAR SURFACES OF FOUR HELIX BUNDLES'''
+
===STRUCTURE BASED ENGINEERING OF INTERNAL MOLECULAR SURFACES OF FOUR HELIX BUNDLES===
-
==Overview==
+
<!--
-
Cavities and clefts are frequently important sites of interaction between natural enzymes or receptors and their corresponding substrate or ligand molecules and exemplify the types of molecular surfaces that would facilitate engineering of artificial catalysts and receptors. Even so, structural characterizations of designed cavities are rare. To address this issue, we performed a systematic study of the structural effects of single-amino acid substitutions within the hydrophobic cores of tetrameric coiled-coil peptides. Peptides containing single glycine, serine, alanine, or threonine amino acid substitutions at the buried L9, L16, L23, and I26 hydrophobic core positions of a GCN4-based sequence were synthesized and studied by solution-phase and crystallographic techniques. All peptides adopt the expected tetrameric state and contain tunnels or internal cavities ranging in size from 80 to 370 A(3). Two closely related sequences containing an L16G substitution, one of which adopts an antiparallel configuration and one of which adopts a parallel configuration, illustrate that cavities of different volumes and shapes can be engineered from identical core substitutions. Finally, we demonstrate that two of the peptides (L9G and L9A) bind the small molecule iodobenzene when present during crystallization, leaving the general peptide quaternary structure intact but altering the local peptide conformation and certain superhelical parameters. These high-resolution descriptions of varied molecular surfaces within solvent-occluded internal cavities illustrate the breadth of design space available in even closely related peptides and offer valuable models for the engineering of de novo helical proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16008357}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16008357 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16008357}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Cavity]]
[[Category: Cavity]]
[[Category: Four helix bundle]]
[[Category: Four helix bundle]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:29:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:22:06 2008''

Revision as of 16:22, 28 July 2008

Image:1uo1.png

Template:STRUCTURE 1uo1

STRUCTURE BASED ENGINEERING OF INTERNAL MOLECULAR SURFACES OF FOUR HELIX BUNDLES

Template:ABSTRACT PUBMED 16008357

About this Structure

1UO1 is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Structure-based engineering of internal cavities in coiled-coil peptides., Yadav MK, Redman JE, Leman LJ, Alvarez-Gutierrez JM, Zhang Y, Stout CD, Ghadiri MR, Biochemistry. 2005 Jul 19;44(28):9723-32. PMID:16008357

Page seeded by OCA on Mon Jul 28 19:22:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uo1"
Personal tools