1cnt
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(New page: 200px<br /> <applet load="1cnt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cnt, resolution 2.4Å" /> '''CILIARY NEUROTROPHIC...)
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Revision as of 14:17, 12 November 2007
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CILIARY NEUROTROPHIC FACTOR
Overview
Ciliary neurotrophic factor (CNTF) promotes the survival and, differentiation of developing motor neurons and is a potential therapeutic, for treating neurodegeneration and nerve injury. The crystal structure of, human CNTF has been determined at 2.4 A resolution using multi-wavelength, anomalous diffraction (MAD) phasing from a single Yb3+ ions. The structure, reveals that CNTF is dimeric, with a novel anti-parallel arrangement of, the subunits, not previously observed for other cytokines. Each subunit, adopts a double crossover four-helix bundle fold, in which two helices, contribute to the dimer interface, whilst two different helices show, pronounced kinks. Analysis of the electrostatic surface of CNTF identified, residues within these kinked helices that may contact the CNTF, receptor-alpha. Solution experiments show that CNTF dimerizes at, concentrations > 40 microM. Such dimers are likely to be relevant to the, storage of CNTF in the peripheral nerve given the high concentrations, present in this tissue. However, it is unlikely that they play a role in, engaging the three distinct receptor subunits that comprise the CNTF, receptor, given the low concentration of extracellular CNTF and its high, potency.
About this Structure
1CNT is a Single protein structure of sequence from Homo sapiens with YB and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing., McDonald NQ, Panayotatos N, Hendrickson WA, EMBO J. 1995 Jun 15;14(12):2689-99. PMID:7796798
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