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.

2l7s

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 19:06, 25 December 2014

Determination of the three-dimensional structure of adrenomedullin, a first step towards the analysis of its interactions with receptors and small molecules

Structural highlights

2l7s is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	2fly
Gene:	ADM, AM (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ADML_HUMAN] AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels.

Publication Abstract from PubMed

Adrenomedullin (AM) is a regulatory peptide which plays many physiological roles including vasodilatation, bronchodilatation, hormone secretion regulation, growth, apoptosis, angiogenesis, and antimicrobial activities, among others. These regulatory activities make AM a relevant player in the pathophysiology of important diseases such as cardiovascular and renal conditions, cancer, and diabetes. Therefore, molecules that target the AM system have been proposed as having therapeutic potential. To guide the design and characterization of such molecules we elucidated the three-dimensional structure of AM in a membrane mimicking medium using NMR spectroscopy methods. Under the employed experimental conditions, the structure can be described as composed by a central alpha-helical region, spanning about one third of its total length, flanked by two disordered segments at both N- and C-termini. The structure of AM in water is completely disordered. The 22-34 region of AM has a general tendency to adopt a helical structure under the employed experimental conditions. Furthermore, the study of the interaction of AM with two of its modulators has also been performed by using chemical shift perturbation analysis NMR methods with 2D-TOCSY experiments, assisted with molecular modelling protocols. We expect these results will help in better understanding the interactions of AM with its receptor and binding proteins/molecules and in the development of novel modulators of AM activities. (c) 2011 Wiley Periodicals, Inc. Biopolymers, 2011.

Structure of micelle-bound adrenomedullin, a first step towards the analysis of its interactions with receptors and small molecules.,Perez-Castells J, Martin-Santamaria S, Nieto L, Ramos A, Martinez A, de Pascual-Teresa B, Jimenez-Barbero J Biopolymers. 2011 Aug 9. doi: 10.1002/bip.21700. PMID:21830197^[1]

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

References

↑ Perez-Castells J, Martin-Santamaria S, Nieto L, Ramos A, Martinez A, de Pascual-Teresa B, Jimenez-Barbero J. Structure of micelle-bound adrenomedullin, a first step towards the analysis of its interactions with receptors and small molecules. Biopolymers. 2011 Aug 9. doi: 10.1002/bip.21700. PMID:21830197 doi:10.1002/bip.21700

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l7s"

@@ Line 8: / Line 8: @@
 <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=2l7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l7s RCSB], [http://www.ebi.ac.uk/pdbsum/2l7s PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ADML_HUMAN ADML_HUMAN]] AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2l7s

From Proteopedia

Revision as of 19:06, 25 December 2014

Determination of the three-dimensional structure of adrenomedullin, a first step towards the analysis of its interactions with receptors and small molecules

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox