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.


1dgv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dgv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1dgv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dgv| PDB=1dgv | SCENE= }}
{{STRUCTURE_1dgv| PDB=1dgv | SCENE= }}
-
'''HOMOLOGY-BASED MODEL OF APO CIB (CALCIUM-AND INTEGRIN-BINDING PROTEIN)'''
+
===HOMOLOGY-BASED MODEL OF APO CIB (CALCIUM-AND INTEGRIN-BINDING PROTEIN)===
-
==Overview==
+
<!--
-
Calcium- and integrin-binding protein (CIB) binds to the 20-residue alphaIIb cytoplasmic domain of platelet alphaIIbbeta3 integrin. Amino acid sequence similarities with calmodulin (CaM) and calcineurin B (CnB) allowed the construction of homology-based models of calcium-saturated CIB as well as apo-CIB. In addition, the solution structure of the alphaIIb cytoplasmic domain in 45% aqueous trifluoroethanol was solved by conventional two-dimensional NMR methods. The models indicate that the N-terminal domain of CIB possesses a number of positively charged residues in its binding site that could interact with the acidic carboxy-terminal LEEDDEEGE sequence of alphaIIb. The C-terminal domain of CIB seems well-suited to bind the sequence WKVGFFKR, which forms a well-structured alpha helix; this is analogous to calmodulin and calcineurin B, which also bind alpha helices. Similarities between the C-terminal domains of CIB and calmodulin suggest that binding of CIB to the cytoplasmic domain of alphaIIb may be affected by fluctuations in the intracellular calcium concentration.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10822252}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10822252 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10822252}}
==About this Structure==
==About this Structure==
-
1DGV is a [[Single protein]] structure of 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=1DGV OCA].
+
1DGV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGV OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Ef-hand]]
[[Category: Ef-hand]]
[[Category: Helical]]
[[Category: Helical]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:50:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:03:55 2008''

Revision as of 20:03, 30 June 2008

Template:STRUCTURE 1dgv

HOMOLOGY-BASED MODEL OF APO CIB (CALCIUM-AND INTEGRIN-BINDING PROTEIN)

Template:ABSTRACT PUBMED 10822252

About this Structure

1DGV is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies., Hwang PM, Vogel HJ, J Mol Recognit. 2000 Mar-Apr;13(2):83-92. PMID:10822252

Page seeded by OCA on Mon Jun 30 23:03:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools