1ij9

From Proteopedia

(Difference between revisions)

Revision as of 11:01, 4 August 2021

Highly Hydrated Human VCAM-1 Fragment

Structural highlights

1ij9 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.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VCAM1_HUMAN] Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.

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

An X-ray crystal structure of two N-terminal integrin-binding IgSF domains of human VCAM-1 is reported. This new crystal form shows an unusual and highly hydrated packing arrangement in which over 80% of the crystal is occupied by solvent. The relative orientations of the two domains adopt a new intermediate conformation. The tilt angle between the two domains is 19.4 degrees, compared with other related structures that have tilt angles ranging from 7.3 to 39.9 degrees. An analysis of the torsion angles shows that residues Ile88, Tyr89, Ser90, Pro92 and Glu96 play a major role in defining the interdomain conformations.

A new conformation of the integrin-binding fragment of human VCAM-1 crystallizes in a highly hydrated packing arrangement.,Taylor P, Bilsland M, Walkinshaw MD Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1579-83. Epub 2001, Oct 25. PMID:11679722^[1]

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

References

↑ Taylor P, Bilsland M, Walkinshaw MD. A new conformation of the integrin-binding fragment of human VCAM-1 crystallizes in a highly hydrated packing arrangement. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1579-83. Epub 2001, Oct 25. PMID:11679722

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/1ij9"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ij9' size='340' side='right'caption='[[1ij9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ij9]] 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=1IJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IJ9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ij9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IJ9 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=1ij9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ij9 OCA], [http://pdbe.org/1ij9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ij9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ij9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ij9 ProSAT]</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=1ij9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ij9 OCA], [https://pdbe.org/1ij9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ij9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ij9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ij9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VCAM1_HUMAN VCAM1_HUMAN]] Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.
+[[https://www.uniprot.org/uniprot/VCAM1_HUMAN VCAM1_HUMAN]] Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ij9

From Proteopedia

Revision as of 11:01, 4 August 2021

Highly Hydrated Human VCAM-1 Fragment

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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