We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1t89

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1t89.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1t89.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t89| PDB=1t89 | SCENE= }}
{{STRUCTURE_1t89| PDB=1t89 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF A HUMAN TYPE III FC GAMMA RECEPTOR IN COMPLEX WITH AN FC FRAGMENT OF IGG1 (HEXAGONAL)'''
+
===CRYSTAL STRUCTURE OF A HUMAN TYPE III FC GAMMA RECEPTOR IN COMPLEX WITH AN FC FRAGMENT OF IGG1 (HEXAGONAL)===
-
==Overview==
+
<!--
-
Fcgamma receptors mediate antibody-dependent inflammatory responses and cytotoxicity as well as certain autoimmune dysfunctions. Here we report the crystal structure of a human Fc receptor (FcgammaRIIIB) in complex with an Fc fragment of human IgG1 determined from orthorhombic and hexagonal crystal forms at 3.0- and 3.5-A resolution, respectively. The refined structures from the two crystal forms are nearly identical with no significant discrepancies between the coordinates. Regions of the C-terminal domain of FcgammaRIII, including the BC, C'E, FG loops, and the C' beta-strand, bind asymmetrically to the lower hinge region, residues Leu(234)-Pro(238), of both Fc chains creating a 1:1 receptor-ligand stoichiometry. Minor conformational changes are observed in both the receptor and Fc upon complex formation. Hydrophobic residues, hydrogen bonds, and salt bridges are distributed throughout the receptor.Fc interface. Sequence comparisons of the receptor-ligand interface residues suggest a conserved binding mode common to all members of immunoglobulin-like Fc receptors. Structural comparison between FcgammaRIII.Fc and FcepsilonRI.Fc complexes highlights the differences in ligand recognition between the high and low affinity receptors. Although not in direct contact with the receptor, the carbohydrate attached to the conserved glycosylation residue Asn(297) on Fc may stabilize the conformation of the receptor-binding epitope on Fc. An antibody-FcgammaRIII model suggests two possible ligand-induced receptor aggregations.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11297532}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11297532 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11297532}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Igg1]]
[[Category: Igg1]]
[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:39:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:28:35 2008''

Revision as of 04:28, 28 July 2008

Image:1t89.png

Template:STRUCTURE 1t89

CRYSTAL STRUCTURE OF A HUMAN TYPE III FC GAMMA RECEPTOR IN COMPLEX WITH AN FC FRAGMENT OF IGG1 (HEXAGONAL)

Template:ABSTRACT PUBMED 11297532

About this Structure

1T89 is a Protein complex structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 1iix. Full crystallographic information is available from OCA.

Reference

The structure of a human type III Fcgamma receptor in complex with Fc., Radaev S, Motyka S, Fridman WH, Sautes-Fridman C, Sun PD, J Biol Chem. 2001 May 11;276(19):16469-77. Epub 2001 Jan 31. PMID:11297532

Page seeded by OCA on Mon Jul 28 07:28:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t89"
Personal tools