2cwb

From Proteopedia

(Difference between revisions)

Revision as of 16:08, 11 September 2015

Solution Structure of the Ubiquitin-Associated Domain of Human BMSC-UbP and its Complex with Ubiquitin

Structural highlights

2cwb is a 1 chain structure with sequence from Strsp. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	BMSC-UbP (STRSP)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ubiquitin is an important cellular signal that targets proteins for degradation or regulates their functions. The previously identified BMSC-UbP protein derived from bone marrow stromal cells contains a ubiquitin-associated (UBA) domain at the C terminus that has been implicated in linking cellular processes and the ubiquitin system. Here, we report the solution NMR structure of the UBA domain of human BMSC-UbP protein and its complex with ubiquitin. The structure determination was facilitated by using a solubility-enhancement tag (SET) GB1, immunoglobulin G binding domain 1 of Streptococcal protein G. The results show that BMSC-UbP UBA domain is primarily comprised of three alpha-helices with a hydrophobic patch defined by residues within the C terminus of helix-1, loop-1, and helix-3. The M-G-I motif is similar to the M/L-G-F/Y motifs conserved in most UBA domains. Chemical shift perturbation study revealed that the UBA domain binds with the conserved five-stranded beta-sheet of ubiquitin via hydrophobic interactions with the dissociation constant (KD) of approximately 17 microM. The structural model of BMSC-UbP UBA domain complexed with ubiquitin was constructed by chemical shift mapping combined with the program HADDOCK, which is in agreement with the result from mutagenesis studies. In the complex structure, three residues (Met76, Ile78, and Leu99) of BMSC-UbP UBA form a trident anchoring the domain to the hydrophobic concave surface of ubiquitin defined by residues Leu8, Ile44, His68, and Val70. This complex structure may provide clues for BMSC-UbP functions and structural insights into the UBA domains of other ubiquitin-associated proteins that share high sequence homology with BMSC-UbP UBA domain.

Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin.,Chang YG, Song AX, Gao YG, Shi YH, Lin XJ, Cao XT, Lin DH, Hu HY Protein Sci. 2006 Jun;15(6):1248-59. PMID:16731964^[1]

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

References

↑ Chang YG, Song AX, Gao YG, Shi YH, Lin XJ, Cao XT, Lin DH, Hu HY. Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin. Protein Sci. 2006 Jun;15(6):1248-59. PMID:16731964 doi:15/6/1248

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cwb"

@@ Line 2: / Line 2: @@
 <StructureSection load='2cwb' size='340' side='right' caption='[[2cwb]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2cwb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CWB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CWB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2cwb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strsp Strsp]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CWB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CWB FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMSC-UbP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1306 Streptococcus sp.])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMSC-UbP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1306 STRSP])</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=2cwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cwb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cwb RCSB], [http://www.ebi.ac.uk/pdbsum/2cwb PDBsum]</span></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=2cwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cwb OCA], [http://pdbe.org/2cwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cwb RCSB], [http://www.ebi.ac.uk/pdbsum/2cwb PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2cwb" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Streptococcus sp]]
+[[Category: Strsp]]
 [[Category: Cao, X T]]
 [[Category: Chang, Y G]]

2cwb

From Proteopedia

Revision as of 16:08, 11 September 2015

Solution Structure of the Ubiquitin-Associated Domain of Human BMSC-UbP and its Complex with Ubiquitin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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