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.


1mm9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mm9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1mm9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mm9| PDB=1mm9 | SCENE= }}
{{STRUCTURE_1mm9| PDB=1mm9 | SCENE= }}
-
'''Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD'''
+
===Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD===
-
==Overview==
+
<!--
-
The RGD (arginine-glycine-aspartic acid) sequence is found in several important extracellular matrix proteins and serves as an adhesion ligand for members of the integrin family of cell-surface receptors. This sequence and flanking residues from fibronectin or osteopontin have been engineered into an accessible surface loop of streptavidin to create two new streptavidin variants (FN-SA or OPN-SA, respectively) that bind cells through the alpha(v)beta(3) and/or alpha(5)beta(1) integrin receptors. Their crystal structures confirm the design and construction of the mutants and provide evidence about the conformational dynamics of the RGD loops. The loops in the isomorphous crystal structures are involved in crystal-packing interactions and this stabilizes their structures. Even so, the loop in OPN-SA is slightly disordered and two of the residues are not seen in difference electron-density maps. Comparison with other experimentally determined structures of RGD loops in cell-adhesion molecules shows that these loops occupy a large subset of conformational space. This is consistent with the view that RGD loops, at least those involved in cell adhesion, sample a number of structures dynamically, a few of which display high affinity for appropriate receptors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12777798}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12777798 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12777798}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Trong, I Le.]]
[[Category: Trong, I Le.]]
[[Category: Tetramer]]
[[Category: Tetramer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:24:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:19:42 2008''

Revision as of 21:19, 2 July 2008

Image:1mm9.png

Template:STRUCTURE 1mm9

Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD

Template:ABSTRACT PUBMED 12777798

About this Structure

1MM9 is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.

Reference

Structural characterization and comparison of RGD cell-adhesion recognition sites engineered into streptavidin., Le Trong I, McDevitt TC, Nelson KE, Stayton PS, Stenkamp RE, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):828-34. Epub 2003, Apr 25. PMID:12777798

Page seeded by OCA on Thu Jul 3 00:19:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mm9"
Personal tools