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.


1pga

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1pga.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1pga.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pga| PDB=1pga | SCENE= }}
{{STRUCTURE_1pga| PDB=1pga | SCENE= }}
-
'''TWO CRYSTAL STRUCTURES OF THE B1 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G AND COMPARISON WITH NMR'''
+
===TWO CRYSTAL STRUCTURES OF THE B1 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G AND COMPARISON WITH NMR===
-
==Overview==
+
<!--
-
The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular replacement, based on the structure of the B2 domain (Brookhaven accession code 1PGX). Final R values are 0.174 and 0.198 for orthorhombic and trigonal forms, for diffraction data from 6.0 to 2.07 A and from 6 to 1.92 A, respectively. The orthorhombic crystals have an unusually high packing density for protein crystals, with Vm = 1.66 and a solvent content of 26%. The protein structure is found to be very similar (rms deviation 0.25 A for 56 C alpha's) in the two crystal forms, with an efficiently packed hydrophobic core between a four-stranded beta-sheet and a four-turn alpha-helix. The B1 domain has the same fold and general structure as the B2 domain (rms deviations 0.36 and 0.39 A), despite the six residue differences between them. The crystallographic models differ from NMR-derived models in several local regions, primarily in the loop involving residues 46-51; other significant variations are observed in the helix and in the structure of bound water. The primary crystal contact is the same in both crystal forms, involving both sheet edges to form extended beta-sheets throughout the crystals.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8161530}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8161530 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8161530}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Gilliland, G L.]]
[[Category: Gilliland, G L.]]
[[Category: Immunoglobulin binding protein]]
[[Category: Immunoglobulin binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:03:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:52:56 2008''

Revision as of 07:53, 28 July 2008

Image:1pga.png

Template:STRUCTURE 1pga

TWO CRYSTAL STRUCTURES OF THE B1 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G AND COMPARISON WITH NMR

Template:ABSTRACT PUBMED 8161530

About this Structure

1PGA is a Single protein structure of sequence from Streptococcus sp. gx7805. Full crystallographic information is available from OCA.

Reference

Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR., Gallagher T, Alexander P, Bryan P, Gilliland GL, Biochemistry. 1994 Apr 19;33(15):4721-9. PMID:8161530

Page seeded by OCA on Mon Jul 28 10:52:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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