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1u2h

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Revision as of 07:19, 30 December 2020

X-ray Structure of the N-terminally truncated human APEP-1

Structural highlights

1u2h is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Arotic Preferentially Expressed Gene 1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[SPEG_HUMAN] Autosomal recessive centronuclear myopathy. The disease is caused by mutations affecting the gene represented in this entry.

Function

[SPEG_HUMAN] Isoform 3 may have a role in regulating the growth and differentiation of arterial smooth muscle cells.

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

BACKGROUND: Human Aortic Preferentially Expressed Protein-1 (APEG-1) is a novel specific smooth muscle differentiation marker thought to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). RESULTS: Good quality crystals that were suitable for X-ray crystallographic studies were obtained following the truncation of the 14 N-terminal amino acids of APEG-1, a region predicted to be disordered. The truncated protein (termed DeltaAPEG-1) consists of a single immunoglobulin (Ig) like domain which includes an Arg-Gly-Asp (RGD) adhesion recognition motif. The RGD motif is crucial for the interaction of extracellular proteins and plays a role in cell adhesion. The X-ray structure of DeltaAPEG-1 was determined and was refined to sub-atomic resolution (0.96 A). This is the best resolution for an immunoglobulin domain structure so far. The structure adopts a Greek-key beta-sandwich fold and belongs to the I (intermediate) set of the immunoglobulin superfamily. The residues lying between the beta-sheets form a hydrophobic core. The RGD motif folds into a 310 helix that is involved in the formation of a homodimer in the crystal which is mainly stabilized by salt bridges. Analytical ultracentrifugation studies revealed a moderate dissociation constant of 20 microM at physiological ionic strength, suggesting that APEG-1 dimerisation is only transient in the cell. The binding constant is strongly dependent on ionic strength. CONCLUSION: Our data suggests that the RGD motif might play a role not only in the adhesion of extracellular proteins but also in intracellular protein-protein interactions. However, it remains to be established whether the rather weak dimerisation of APEG-1 involving this motif is physiologically relevant.

X-ray structure of engineered human Aortic Preferentially Expressed Protein-1 (APEG-1).,Manjasetty BA, Niesen FH, Scheich C, Roske Y, Goetz F, Behlke J, Sievert V, Heinemann U, Bussow K BMC Struct Biol. 2005 Dec 14;5:21. PMID:16354304^[1]

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

References

↑ Manjasetty BA, Niesen FH, Scheich C, Roske Y, Goetz F, Behlke J, Sievert V, Heinemann U, Bussow K. X-ray structure of engineered human Aortic Preferentially Expressed Protein-1 (APEG-1). BMC Struct Biol. 2005 Dec 14;5:21. PMID:16354304 doi:10.1186/1472-6807-5-21

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u2h"

@@ Line 1: / Line 1: @@
 ==X-ray Structure of the N-terminally truncated human APEP-1==
-<StructureSection load='1u2h' size='340' side='right' caption='[[1u2h]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
+<StructureSection load='1u2h' size='340' side='right'caption='[[1u2h]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u2h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U2H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u2h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1U2H FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Arotic Preferentially Expressed Gene 1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1u2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2h OCA], [http://pdbe.org/1u2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u2h RCSB], [http://www.ebi.ac.uk/pdbsum/1u2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2h ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1u2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2h OCA], [http://pdbe.org/1u2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u2h RCSB], [http://www.ebi.ac.uk/pdbsum/1u2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2h ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Bussow, K]]
 [[Category: Gotz, F]]

1u2h

From Proteopedia

Revision as of 07:19, 30 December 2020

X-ray Structure of the N-terminally truncated human APEP-1

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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