2jw6
From Proteopedia
(New page: 200px<br /><applet load="2jw6" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jw6" /> '''Solution structure of the DEAF1 MYND domain'...) |
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==Overview== | ==Overview== | ||
| - | The MYND domain (named after myeloid translocation protein 8, Nervy, and | + | The MYND domain (named after myeloid translocation protein 8, Nervy, and DEAF-1) is a conserved zinc binding domain. It is defined by seven conserved cysteine residues and a single histidine residue that are arranged in a C4-C2HC consensus. MYND domains exist in a large number of proteins that play important roles in development or are associated with cancers and have been shown to mediate protein-protein interactions, mainly in the context of transcriptional regulation. We have determined the three-dimensional structure of the MYND domain from human deformed epidermal autoregulatory factor-1 (DEAF-1). The structure reveals a novel zinc binding fold, in which the C4-C2HC motif forms two sequential zinc binding sites. The first and second zinc binding modules comprise a small beta hairpin and two short alpha helices, respectively. The sequential topology of the two zinc binding sites is distinct from the cross-brace PHD and RING finger folds but has some resemblance to LIM domains. The structure reveals that the MYND domain is a novel member of the treble-clef family of zinc binding domains. The MYND domains of BS69 and BOP bind ligands comprising a PXLXP peptide motif. On the basis of the solution structure of the DEAF-1 MYND domain we calculated a homology model of the MYND domain of the BS69 tumor suppressor. A mutational analysis of the BS69 MYND domain indicates that positively charged residues located on one face of its MYND domain are crucial for the molecular interactions of BS69. Different binding specificities of MYND domains may depend on distinct surface charge distributions. |
==About this Structure== | ==About this Structure== | ||
| - | 2JW6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 2JW6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 2FV6. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JW6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:16 2008'' |
Revision as of 16:06, 21 February 2008
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Solution structure of the DEAF1 MYND domain
Overview
The MYND domain (named after myeloid translocation protein 8, Nervy, and DEAF-1) is a conserved zinc binding domain. It is defined by seven conserved cysteine residues and a single histidine residue that are arranged in a C4-C2HC consensus. MYND domains exist in a large number of proteins that play important roles in development or are associated with cancers and have been shown to mediate protein-protein interactions, mainly in the context of transcriptional regulation. We have determined the three-dimensional structure of the MYND domain from human deformed epidermal autoregulatory factor-1 (DEAF-1). The structure reveals a novel zinc binding fold, in which the C4-C2HC motif forms two sequential zinc binding sites. The first and second zinc binding modules comprise a small beta hairpin and two short alpha helices, respectively. The sequential topology of the two zinc binding sites is distinct from the cross-brace PHD and RING finger folds but has some resemblance to LIM domains. The structure reveals that the MYND domain is a novel member of the treble-clef family of zinc binding domains. The MYND domains of BS69 and BOP bind ligands comprising a PXLXP peptide motif. On the basis of the solution structure of the DEAF-1 MYND domain we calculated a homology model of the MYND domain of the BS69 tumor suppressor. A mutational analysis of the BS69 MYND domain indicates that positively charged residues located on one face of its MYND domain are crucial for the molecular interactions of BS69. Different binding specificities of MYND domains may depend on distinct surface charge distributions.
About this Structure
2JW6 is a Single protein structure of sequence from Homo sapiens with as ligand. This structure supersedes the now removed PDB entry 2FV6. Full crystallographic information is available from OCA.
Reference
Structure and functional analysis of the MYND domain., Spadaccini R, Perrin H, Bottomley MJ, Ansieau S, Sattler M, J Mol Biol. 2006 Apr 28;358(2):498-508. Epub 2006 Feb 8. PMID:16527309
Page seeded by OCA on Thu Feb 21 18:06:16 2008
Categories: Homo sapiens | Single protein | Ansieu, S. | Bottomley, M. | Perrin, H. | Sattler, M. | Spadaccini, R. | ZN | Alternative splicing | Disease mutation | Dna-binding | Metal-binding | Nucleus | Phosphorylation | Secreted | Transcription | Transcription regulation | Zinc binding domain | Zinc-finger
