This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1u2h

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

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

Structural highlights

1u2h is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 0.96Å
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/Homo_sapiens Homo sapiens]. 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 [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1U2H FirstGlance]. <br>
-</td></tr><tr><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 Homo sapiens])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.96&#8491;</td></tr>
-<tr><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://www.rcsb.org/pdb/explore.do?structureId=1u2h RCSB], [http://www.ebi.ac.uk/pdbsum/1u2h PDBsum]</span></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=1u2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2h OCA], [https://pdbe.org/1u2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2h RCSB], [https://www.ebi.ac.uk/pdbsum/1u2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2h ProSAT]</span></td></tr>
-<table>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/SPEG_HUMAN SPEG_HUMAN] Autosomal recessive centronuclear myopathy. The disease is caused by mutations affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/SPEG_HUMAN SPEG_HUMAN] Isoform 3 may have a role in regulating the growth and differentiation of arterial smooth muscle cells.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u2h_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u2h_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1u2h ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 24: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1u2h" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 29: / Line 35: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Bussow, K.]]
+[[Category: Large Structures]]
-[[Category: Gotz, F.]]
+[[Category: Bussow K]]
-[[Category: Heinemann, U.]]
+[[Category: Gotz F]]
-[[Category: Manjasetty, B A.]]
+[[Category: Heinemann U]]
-[[Category: Niesen, F H.]]
+[[Category: Manjasetty BA]]
-[[Category: Roske, Y.]]
+[[Category: Niesen FH]]
-[[Category: Scheich, C.]]
+[[Category: Roske Y]]
-[[Category: Arterial smooth muscle cell]]
+[[Category: Scheich C]]
-[[Category: Atherosclerosis]]
-[[Category: Contractile protein]]
-[[Category: Homophilic adhesion]]
-[[Category: Ig-fold i-set]]
-[[Category: Rgd motif]]
-[[Category: Structural genomic]]

1u2h

From Proteopedia

Current revision

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

Personal tools

Navigation

Search

Toolbox