1dok

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(New page: 200px<br /> <applet load="1dok" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dok, resolution 1.85&Aring;" /> '''MONOCYTE CHEMOATTRA...)
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Revision as of 14:28, 12 November 2007


1dok, resolution 1.85Å

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MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM

Contents

Overview

The X-ray crystal structure of recombinant human monocyte chemoattractant, protein (MCP-1) has been solved in two crystal forms. One crystal form, (P), refined to 1.85 A resolution, contains a dimer in the asymmetric, unit, while the other (I) contains a monomer and was refined at 2.4 A., Although both crystal forms grow together in the same droplet, the, respective quaternary structures of the protein differ dramatically. In, addition, both X-ray structures differ to a similar extent from the, solution structure of MCP-1. Such extent of variability of quaternary, structures is unprecedented. In the crystal structures, the well-ordered N, termini of MCP-1 form 3(10)-helices. Comparison of the three MCP-1, structures revealed a direct correlation between the main-chain, conformation of the first two cysteine residues and the quaternary, arrangements. These data can be used to explain the structural basis for, the assignment of residues responsible for biological activity.

Disease

Known diseases associated with this structure: Coronary artery disease, modifier of OMIM:[158105], HIV-1, resistance to OMIM:[158105], Mycobacterium tuberculosis, susceptibility to OMIM:[158105], Spina bifida, susceptiblity to OMIM:[158105]

About this Structure

1DOK is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions., Lubkowski J, Bujacz G, Boque L, Domaille PJ, Handel TM, Wlodawer A, Nat Struct Biol. 1997 Jan;4(1):64-9. PMID:8989326

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