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.


2q7z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2q7z.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2q7z.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2q7z| PDB=2q7z | SCENE= }}
{{STRUCTURE_2q7z| PDB=2q7z | SCENE= }}
-
'''Solution Structure of the 30 SCR domains of human Complement Receptor 1'''
+
===Solution Structure of the 30 SCR domains of human Complement Receptor 1===
-
==Overview==
+
<!--
-
Human complement receptor type 1 (CR1, CD35) is a type I membrane-bound glycoprotein that belongs to the regulators of complement activity (RCA) family. The extra-cellular component of CR1 is comprised of 30 short complement regulator (SCR) domains, whereas complement receptor type 2 (CR2) has 15 SCR domains and factor H (FH) has 20 SCR domains. The domain arrangement of a soluble form of CR1 (sCR1) was studied by X-ray scattering and analytical ultracentrifugation. The radius of gyration R(G) of sCR1 of 13.4(+/-1.1) nm is not much greater than those for CR2 and FH, and its R(G)/R(0) anisotropy ratio is 3.76, compared to ratios of 3.67 for FH and 4.1 for CR2. Unlike CR2, but similar to FH, two cross-sectional R(G) ranges were identified that gave R(XS) values of 4.7(+/-0.2) nm and 1.2(+/-0.7) nm, respectively, showing that the SCR domains adopt a range of conformations including folded-back ones. The distance distribution function P(r) showed that the most commonly occurring distance in sCR1 is at 11.5 nm. Its maximum length of 55 nm is less than double those for CR2 or FH, even though sCR1 has twice the number of SCR domains compared to CR2 Sedimentation equilibrium experiments gave a mean molecular weight of 235 kDa for sCR1. This is consistent with the value of 245 kDa calculated from its composition including 14 N-linked oligosaccharide sites, and confirmed that sCR1 is a monomer in solution. Sedimentation velocity experiments gave a sedimentation coefficient of 5.8 S. From this, the frictional ratio (f/f(0)) of sCR1 was calculated to be 2.29, which is greater than those of 1.96 for CR2 and 1.77 for FH. The constrained scattering modelling of the sCR1 solution structure starting from homologous SCR domain structures generated 5000 trial conformationally randomised models, 43 of which gave good scattering fits to show that sCR1 has a partly folded-back structure. We conclude that the inter-SCR linkers show structural features in common with those in FH, but differ from those in CR2, and the SCR arrangement in CR1 will permit C3b or C4b to access all three ligand sites.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18028942}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18028942 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18028942}}
==About this Structure==
==About this Structure==
Line 42: Line 46:
[[Category: Sushi]]
[[Category: Sushi]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:30:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:54:18 2008''

Revision as of 04:54, 29 July 2008

Image:2q7z.png

Template:STRUCTURE 2q7z

Solution Structure of the 30 SCR domains of human Complement Receptor 1

Template:ABSTRACT PUBMED 18028942

About this Structure

2Q7Z is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The partly folded back solution structure arrangement of the 30 SCR domains in human complement receptor type 1 (CR1) permits access to its C3b and C4b ligands., Furtado PB, Huang CY, Ihyembe D, Hammond RA, Marsh HC, Perkins SJ, J Mol Biol. 2008 Jan 4;375(1):102-18. Epub 2007 Oct 3. PMID:18028942

Page seeded by OCA on Tue Jul 29 07:54:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2q7z"
Personal tools