1bw6

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(Difference between revisions)

Revision as of 07:02, 24 February 2021

HUMAN CENTROMERE PROTEIN B (CENP-B) DNA BINDIGN DOMAIN RP1

Structural highlights

1bw6 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[CENPB_HUMAN] Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.

Publication Abstract from PubMed

CENP-B has been suggested to organize arrays of centromere satellite DNA into a higher order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes. The N-terminal portion of CENP-B is a 15 kDa DNA binding domain (DBD) consisting of two repeating units, RP1 and RP2. The DBD specifically binds to the CENP-B box sequence (17 bp) in centromere DNA. We determined the solution structure of human CENP-B DBD RP1 by multi-dimensional 1H, 13C and 15N NMR methods. The CENP-B DBD RP1 structure consists of four helices and has a helix-turn-helix structure. The overall folding is similar to those of some other eukaryotic DBDs, although significant sequence homology with these proteins was not found. The DBD of yeast RAP1, a telomere binding protein, is most similar to CENP-B DBD RP1. We studied the interaction between CENP-B DBD RP1 and the CENP-B box by the use of NMR chemical shift perturbation. The results suggest that CENP-B DBD RP1 interacts with one of the essential regions of the CENP-B box DNA, mainly at the N-terminal basic region, the N-terminal portion of helix 2 and helix 3.

A helix-turn-helix structure unit in human centromere protein B (CENP-B).,Iwahara J, Kigawa T, Kitagawa K, Masumoto H, Okazaki T, Yokoyama S EMBO J. 1998 Feb 2;17(3):827-37. PMID:9451007^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Iwahara J, Kigawa T, Kitagawa K, Masumoto H, Okazaki T, Yokoyama S. A helix-turn-helix structure unit in human centromere protein B (CENP-B). EMBO J. 1998 Feb 2;17(3):827-37. PMID:9451007 doi:http://dx.doi.org/10.1093/emboj/17.3.827

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bw6"

@@ Line 3: / Line 3: @@
 <StructureSection load='1bw6' size='340' side='right'caption='[[1bw6]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bw6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BW6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bw6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BW6 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bw6 OCA], [http://pdbe.org/1bw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bw6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bw6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bw6 ProSAT], [http://www.topsan.org/Proteins/RSGI/1bw6 TOPSAN]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bw6 OCA], [https://pdbe.org/1bw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bw6 RCSB], [https://www.ebi.ac.uk/pdbsum/1bw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bw6 ProSAT], [https://www.topsan.org/Proteins/RSGI/1bw6 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CENPB_HUMAN CENPB_HUMAN]] Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.
+[[https://www.uniprot.org/uniprot/CENPB_HUMAN CENPB_HUMAN]] Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

1bw6

From Proteopedia

Revision as of 07:02, 24 February 2021

HUMAN CENTROMERE PROTEIN B (CENP-B) DNA BINDIGN DOMAIN RP1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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